Structural highlights
3vom is a 2 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Related: | 2fyf |
| Gene: | MT0907, MTCY31.12c, Rv0884c, serC ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) |
| Activity: | Phosphoserine transaminase, with EC number 2.6.1.52 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[SERC_MYCTU] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).[HAMAP-Rule:MF_00160]
Publication Abstract from PubMed
Mycobacterium tuberculosis (Mtb), the causative agent of TB, remains a serious world health problem owing to limitations of the available drugs and the emergence of resistant strains. In this context, key biosynthetic enzymes from Mtb are attractive targets for the development of new therapeutic drugs. Here, the 1.5 A resolution crystal structure of Mtb phosphoserine aminotransferase (MtbPSAT) in complex with its cofactor, pyridoxal 5'-phosphate (PLP), is reported. MtbPSAT is an essential enzyme in the biosynthesis of serine and in pathways of one-carbon metabolism. The structure shows that although the Mtb enzyme differs substantially in sequence from other PSAT enzymes, its fold is conserved and its PLP-binding site is virtually identical. Structural comparisons suggest that this site remains unchanged throughout the catalytic cycle. On the other hand, PSAT enzymes are obligate dimers in which the two active sites are located in the dimer interface and distinct differences in the MtbPSAT dimer are noted. These impact on the substrate-binding region and access channel and suggest options for the development of selective inhibitors.
Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis.,Coulibaly F, Lassalle E, Baker HM, Baker EN Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):553-63. Epub 2012 Apr 17. PMID:22525753[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Coulibaly F, Lassalle E, Baker HM, Baker EN. Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):553-63. Epub 2012 Apr 17. PMID:22525753 doi:10.1107/S0907444912004829
