Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target for anti-tuberculosis agents development | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
gene Rv2606c, recombinant expression of N-terminally His6-tagged enzyme with a TEV protease cleavage site in Escherichia coli strain B834 | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
H170N | site-directed mutagenesis | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WII9 | gene Rv2606c | - |
Mycobacterium tuberculosis H37Rv | P9WII9 | gene Rv2606c | - |
Purification (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
PdxS | - |
Mycobacterium tuberculosis |
pyridoxal biosynthesis lyase | - |
Mycobacterium tuberculosis |
Rv2606c | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
malfunction | the disruption of the PdxS gene generates a vitamin B6 auxotrophic Mycobacterium tuberculosis mutant | Mycobacterium tuberculosis |
metabolism | the organism synthesizes pyridoxal 5'-phosphate via the deoxyxylulose 5-phosphate (DXP)-dependent pathway | Mycobacterium tuberculosis |
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 |
physiological function | vitamin B6 biosynthesis is essential for the survival and virulence of Mycobacterium tuberculosis | Mycobacterium tuberculosis |