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Literature summary extracted from

  • Kim, S.; Kim, K.J.
    Crystal structure of Mycobacterium tuberculosis Rv2606c: a pyridoxal biosynthesis lyase (2013), Biochem. Biophys. Res. Commun., 435, 255-259.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.3.3.6 drug development the enzyme is a target for anti-tuberculosis agents development Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.6 gene Rv2606c, recombinant expression of N-terminally His6-tagged enzyme with a TEV protease cleavage site in Escherichia coli strain B834 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.6 purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 00.0015 ml of 22 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 5 mM 2-mercaptoethanol, with 0.0015 ml of reservoir solution, containing 8% PEG 8000, 0.1 M 3-[cyclohexylamino]-1-propanesulfonic acid, pH 10.5, and 0.2 M sodium chloride, and equilibration against 0.5 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using the Thermotoga maritima PdxS, PDB code 2ISS Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
4.3.3.6 H170N site-directed mutagenesis Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.3.6 additional information a glycerol molecule is bound at the active site of the enzyme structure through interactions with the conserved residues of Asp29 and Lys86 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.6 Mycobacterium tuberculosis P9WII9 gene Rv2606c
-
4.3.3.6 Mycobacterium tuberculosis H37Rv P9WII9 gene Rv2606c
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.6 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain B834 by nickel affinity chromatography and cleavage of the tag by TEV protease, followed by anion exchange chromatography and gel filtration to about 95% purity Mycobacterium tuberculosis

Subunits

EC Number Subunits Comment Organism
4.3.3.6 More from crystal structure, the asymmetric unit contains 3 Rv2606c molecules, and the dodecameric structure of the protein can be generated by applying crystallographic I222 symmetry, interfaces for the formation of dodecameric structure, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
4.3.3.6 PdxS
-
 Mycobacterium tuberculosis
4.3.3.6 pyridoxal biosynthesis lyase
-
 Mycobacterium tuberculosis
4.3.3.6 Rv2606c
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
4.3.3.6 malfunction the disruption of the PdxS gene generates a vitamin B6 auxotrophic Mycobacterium tuberculosis mutant Mycobacterium tuberculosis
4.3.3.6 metabolism the organism synthesizes pyridoxal 5'-phosphate via the deoxyxylulose 5-phosphate (DXP)-dependent pathway Mycobacterium tuberculosis
4.3.3.6 additional information the overall structure of the protein, composed of a (beta/alpha)8-barrel and two small 310-helices, is quite similar to those of other PdxS proteins. Rv2606c and Rv2604c form a stable complex, suggesting that these proteins might function as pyridoxal biosynthesis lyase and glutamine amidotransferase, respectively Mycobacterium tuberculosis
4.3.3.6 physiological function vitamin B6 biosynthesis is essential for the survival and virulence of Mycobacterium tuberculosis Mycobacterium tuberculosis