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show all sequences of 7.6.2.5

Structural basis for heme recognition by HmuT responsible for heme transport to the heme transporter in Corynebacterium glutamicum

Muraki, N.; Aono, S.; Chem. Lett. 45, 24-26 (2016)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene hmuT, lactose-inducible recombinant expression of His-tagged HmuT in Escherichia coli strain BL21(DE3)
Corynebacterium glutamicum
Crystallization (Commentary)
Crystallization
Organism
purified recombinant His-tagged purified CgHmuT from enzyme complex HmuTUV in the holo-form, hanging drop vapour diffusion method, mixing of 50 mg/ml protein in 50 mM Tris-HCl, pH 8.5, and 200 mM NaCl with precipitant solution containing 2.1 M ammonium sulfate and 0.2 M potassium thiocyanate, X-ray diffraction structure determination and analysis at 1.42 A resolution
Corynebacterium glutamicum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
inner membrane
periplasmic heme-binding protein HmuT binds heme to transport it to an ABC-type heme transporter, which transports it through the inner membrane to the cytoplasm
Corynebacterium glutamicum
-
-
periplasm
periplasmic heme-binding protein HmuT binds heme to transport it to an ABC-type heme transporter
Corynebacterium glutamicum
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + heme[side 1]
Corynebacterium glutamicum
-
ADP + phosphate + heme[side 2]
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium glutamicum
A0A160PR71 AND A0A160PQ30 AND A0A169RPR0
ABC-type heme transporter system HmuTUV encoded by genes hmut, hmuu, and hmuv
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged HmuT from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, followed by gel filtration and unltrafiltration, HmuT is obtained in holo-form
Corynebacterium glutamicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + heme[side 1]
-
750302
Corynebacterium glutamicum
ADP + phosphate + heme[side 2]
-
-
-
?
additional information
there is a cleft between the N- and C-terminal domains, in which one heme molecule is accommodated with His141 and Tyr240 as axial ligands that are located at the loop regions in the N- and C-terminal domains, respectively. The Fe-N and Fe-O bond distances are 2.2 and 2.1 A, respectively. Heme is accommodated in the heme-binding site of CgHmuT with two different orientations
750302
Corynebacterium glutamicum
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
there is a cleft between the N- and C-terminal domains, in which one heme molecule is accommodated with His141 and Tyr240 as axial ligands that are located at the loop regions in the N- and C-terminal domains, respectively. The Fe-N and Fe-O bond distances are 2.2 and 2.1 A, respectively. Heme-binding protein structure comparisons, overview
Corynebacterium glutamicum
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Corynebacterium glutamicum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene hmuT, lactose-inducible recombinant expression of His-tagged HmuT in Escherichia coli strain BL21(DE3)
Corynebacterium glutamicum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Corynebacterium glutamicum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant His-tagged purified CgHmuT from enzyme complex HmuTUV in the holo-form, hanging drop vapour diffusion method, mixing of 50 mg/ml protein in 50 mM Tris-HCl, pH 8.5, and 200 mM NaCl with precipitant solution containing 2.1 M ammonium sulfate and 0.2 M potassium thiocyanate, X-ray diffraction structure determination and analysis at 1.42 A resolution
Corynebacterium glutamicum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
inner membrane
periplasmic heme-binding protein HmuT binds heme to transport it to an ABC-type heme transporter, which transports it through the inner membrane to the cytoplasm
Corynebacterium glutamicum
-
-
periplasm
periplasmic heme-binding protein HmuT binds heme to transport it to an ABC-type heme transporter
Corynebacterium glutamicum
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + heme[side 1]
Corynebacterium glutamicum
-
ADP + phosphate + heme[side 2]
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged HmuT from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, followed by gel filtration and unltrafiltration, HmuT is obtained in holo-form
Corynebacterium glutamicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + heme[side 1]
-
750302
Corynebacterium glutamicum
ADP + phosphate + heme[side 2]
-
-
-
?
additional information
there is a cleft between the N- and C-terminal domains, in which one heme molecule is accommodated with His141 and Tyr240 as axial ligands that are located at the loop regions in the N- and C-terminal domains, respectively. The Fe-N and Fe-O bond distances are 2.2 and 2.1 A, respectively. Heme is accommodated in the heme-binding site of CgHmuT with two different orientations
750302
Corynebacterium glutamicum
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
there is a cleft between the N- and C-terminal domains, in which one heme molecule is accommodated with His141 and Tyr240 as axial ligands that are located at the loop regions in the N- and C-terminal domains, respectively. The Fe-N and Fe-O bond distances are 2.2 and 2.1 A, respectively. Heme-binding protein structure comparisons, overview
Corynebacterium glutamicum
General Information
General Information
Commentary
Organism
additional information
substrate heme is accommodated with two different orientations in the central cleft of the HmuTUV complex protein CgHmuT, in which His141 and Tyr240 are coordinated to the heme as axial ligands
Corynebacterium glutamicum
physiological function
HmuT from Corynebacterium glutamicum is a heme-binding protein in an ABC-type heme transporter system, HmuTUV. The Corynebacterium glutamicum heme acquisition system consists of HtaA, HtaB, and HmuTUV. Heme is transported into the cytoplasm by this ABC transporter. Heme is captured by the membrane-anchored heme-binding proteins, HtaA and HtaB, and is transferred to HmuT, which is a heme-binding protein for the ABC-type heme transporter HmuUV. Pathogenic bacteria use heme as an iron source partly because heme is the most abundant iron species in their host
Corynebacterium glutamicum
General Information (protein specific)
General Information
Commentary
Organism
additional information
substrate heme is accommodated with two different orientations in the central cleft of the HmuTUV complex protein CgHmuT, in which His141 and Tyr240 are coordinated to the heme as axial ligands
Corynebacterium glutamicum
physiological function
HmuT from Corynebacterium glutamicum is a heme-binding protein in an ABC-type heme transporter system, HmuTUV. The Corynebacterium glutamicum heme acquisition system consists of HtaA, HtaB, and HmuTUV. Heme is transported into the cytoplasm by this ABC transporter. Heme is captured by the membrane-anchored heme-binding proteins, HtaA and HtaB, and is transferred to HmuT, which is a heme-binding protein for the ABC-type heme transporter HmuUV. Pathogenic bacteria use heme as an iron source partly because heme is the most abundant iron species in their host
Corynebacterium glutamicum
Other publictions for EC 7.6.2.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750302
Muraki
-
Structural basis for heme rec ...
Corynebacterium glutamicum
Chem. Lett.
45
24-26
2016
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289166
Schulz
Heme transfer to the heme chap ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
96
6462-6467
1999
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289160
Goldman
Transmembrane heme delivery sy ...
Bacillus subtilis, Bradyrhizobium japonicum, Escherichia coli, Haemophilus influenzae, Marchantia sp., Mycobacterium leprae, Mycobacterium tuberculosis, Paracoccus denitrificans, Porphyra sp., Pseudomonas fluorescens, Rhodobacter capsulatus
Proc. Natl. Acad. Sci. USA
95
5003-5008
1998
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289163
Keightley
Cloning and expression in Esch ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biol. Chem.
273
12006-12016
1998
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289161
Goldman
Use of heme reporters for stud ...
Escherichia coli
J. Bacteriol.
178
6338-6347
1996
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289165
Nakazono
The gene for a subunit of an A ...
Oryza sativa, Rhodobacter capsulatus
Curr. Genet.
29
412-416
1996
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289162
Jekabsons
orf250 encodes a second subuni ...
Arabidopsis thaliana, Daucus carota, Escherichia coli, Oenothera berteroana
Mol. Gen. Genet.
246
166-173
1995
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289167
Schuster
The highly edited orf206 in Oe ...
Arabidopsis thaliana, Daucus carota, Oenothera berteroana
Plant Mol. Biol.
25
33-42
1994
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289164
Ramseier
Discovery and sequence analysi ...
Bradyrhizobium japonicum
J. Biol. Chem.
266
7793-7803
1991
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