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show all sequences of 2.3.1.191

Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis

Bartling, C.M.; Raetz, C.R.; Biochemistry 48, 8672-8683 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
LpxD protein modified with an N-terminal His6 tag followed by a one glycine residue linker and the P2A substitution, is constructed and transformed into Escherichia coli Rosetta (DE3)/pLysS
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
hanging drop/vapor diffusion method. The crystal structure of N-terminally His6-tagged EcLpxD is determined by molecular replacement at 2.6 A resolution, using Chlamydia trachomatis (PDB code: 2IUA) as the model. Comparison of LpxD from Escherichia coli and Chlamydia trachomatis. Attempts to crystallize EcLpxD with UDP-GlcNAc, UDP-3-O-(R-3-hydroxymyristoyl)-R-D-GlcNAc or its product UDP-2,3-diacylglucosamine are unsuccessful
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
M290A
wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, whereas the M290A mutant has the opposite selectivity. Both wild-type and M290A EcLpxD rescue the conditional lethality of Escherichia coli RL25, a temperature-sensitive strain harboring point mutations in lpxD. Complementation with wild-type EcLpxD restores normal lipid A containing only N-linked hydroxymyristate to RL25 at 42°C, as judged by mass spectrometry, whereas the M290A mutant generates multiple lipid A species containing one or two longer hydroxy fatty acids in place of the usual (3R)-3-hydroxymyristate at positions 2 and 20
Escherichia coli
M292A
wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, mutant enzyme M292A prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 2.5
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P21645
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R,S)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity
696356
Escherichia coli
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
-
-
?
(R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity
696356
Escherichia coli
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
LpxD protein modified with an N-terminal His6 tag followed by a one glycine residue linker and the P2A substitution, is constructed and transformed into Escherichia coli Rosetta (DE3)/pLysS
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging drop/vapor diffusion method. The crystal structure of N-terminally His6-tagged EcLpxD is determined by molecular replacement at 2.6 A resolution, using Chlamydia trachomatis (PDB code: 2IUA) as the model. Comparison of LpxD from Escherichia coli and Chlamydia trachomatis. Attempts to crystallize EcLpxD with UDP-GlcNAc, UDP-3-O-(R-3-hydroxymyristoyl)-R-D-GlcNAc or its product UDP-2,3-diacylglucosamine are unsuccessful
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
M290A
wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, whereas the M290A mutant has the opposite selectivity. Both wild-type and M290A EcLpxD rescue the conditional lethality of Escherichia coli RL25, a temperature-sensitive strain harboring point mutations in lpxD. Complementation with wild-type EcLpxD restores normal lipid A containing only N-linked hydroxymyristate to RL25 at 42°C, as judged by mass spectrometry, whereas the M290A mutant generates multiple lipid A species containing one or two longer hydroxy fatty acids in place of the usual (3R)-3-hydroxymyristate at positions 2 and 20
Escherichia coli
M292A
wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, mutant enzyme M292A prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 2.5
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R,S)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity
696356
Escherichia coli
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
-
-
?
(R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity
696356
Escherichia coli
UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
-
-
-
?
Other publictions for EC 2.3.1.191
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)
735568
Alshalchi
Expression of the lipopolysacc ...
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Arch. Microbiol.
197
135-145
2015
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736235
Eshghi
Leptospira interrogans lpxD ho ...
Leptospira interrogans, Leptospira interrogans L495
Infect. Immun.
83
4314-4321
2015
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736449
Jenkins
Structural basis for the recog ...
Escherichia coli
J. Biol. Chem.
289
15527-15535
2014
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736880
Masoudi
Chasing acyl carrier protein t ...
Escherichia coli
Nature
505
422-426
2014
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1
1
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737072
Emiola
A complete pathway model for l ...
Escherichia coli
PLoS ONE
10
e0121216
2014
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1
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735384
Badger
Structure determination of Lpx ...
Acinetobacter baumannii, Acinetobacter baumannii SDF
Acta Crystallogr. Sect. F
69
6-9
2013
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736185
Yeom
Pleiotropic effects of acyltra ...
Pseudomonas aeruginosa
Genes Cells
18
682-693
2013
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718571
Jenkins
A continuous fluorescent enzym ...
Escherichia coli
Anal. Biochem.
425
21-27
2012
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720944
Li
LPS remodeling is an evolved s ...
Francisella tularensis subsp. novicida, Francisella tularensis subsp. novicida U112
Proc. Natl. Acad. Sci. USA
109
8716-8721
2012
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3
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718513
Badger
The structure of LpxD from Pse ...
Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
67
749-752
2011
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720913
Li
Pathway for lipid A biosynthes ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Proc. Natl. Acad. Sci. USA
108
11387-11392
2011
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696356
Bartling
Crystal structure and acyl cha ...
Escherichia coli
Biochemistry
48
8672-8683
2009
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696264
Bartling
Steady-state kinetics and mech ...
Escherichia coli
Biochemistry
47
5290-5302
2008
1
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1
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10
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8
21
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1
1
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1
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7
21
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11
698587
Bainbridge
Acyl chain specificity of the ...
Escherichia coli, Porphyromonas gingivalis
J. Bacteriol.
190
4549-4558
2008
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694027
Albers
Expression of Legionella pneum ...
Legionella pneumophila
Microbiology
153
3817-3829
2007
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700935
Buetow
Structure and reactivity of Lp ...
Chlamydia trachomatis
Proc. Natl. Acad. Sci. USA
104
4321-4326
2007
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695627
Vaara
Outer membrane permeability ba ...
Escherichia coli
Antimicrob. Agents Chemother.
43
1459-1462
1999
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698088
Steeghs
Isolation and characterization ...
Neisseria meningitidis
Gene
190
263-270
1997
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697921
Vuorio
The novel hexapeptide motif fo ...
Yersinia enterocolitica
FEBS Lett.
337
289-292
1994
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698693
Kelly
Raetz, C.R.; Anderson, M.S.: T ...
Escherichia coli
J. Biol. Chem.
268
19866-19874
1993
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