1oy0
From Proteopedia
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'''The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping''' | '''The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping''' | ||
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[[Category: Waldo, G S.]] | [[Category: Waldo, G S.]] | ||
[[Category: Yeates, T O.]] | [[Category: Yeates, T O.]] | ||
- | [[Category: | + | [[Category: Domain swapping]] |
- | [[Category: | + | [[Category: Protein structure initiative]] |
- | [[Category: | + | [[Category: Psi]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Tb structural genomics consortium]] |
- | [[Category: | + | [[Category: Tbsgc]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:25:02 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 01:25, 3 May 2008
The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping
Overview
Ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first committed step in the biosynthesis of pantothenate, which is a precursor to coenzyme A and is required for penicillin biosynthesis. The crystal structure of KPHMT from Mycobacterium tuberculosis was determined by the single anomalous substitution (SAS) method at 2.8 A resolution. KPHMT adopts a structure that is a variation on the (beta/alpha) barrel fold, with a metal binding site proximal to the presumed catalytic site. The protein forms a decameric complex, with subunits in opposing pentameric rings held together by a swapping of their C-terminal alpha helices. The structure reveals KPHMT's membership in a small, recently discovered group of (beta/alpha) barrel enzymes that employ domain swapping to form a variety of oligomeric assemblies. The apparent conservation of certain detailed structural characteristics suggests that KPHMT is distantly related by divergent evolution to enzymes in unrelated pathways, including isocitrate lyase and phosphoenolpyruvate mutase.
About this Structure
1OY0 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis., Chaudhuri BN, Sawaya MR, Kim CY, Waldo GS, Park MS, Terwilliger TC, Yeates TO, Structure. 2003 Jul;11(7):753-64. PMID:12842039 Page seeded by OCA on Sat May 3 04:25:02 2008
Categories: 3-methyl-2-oxobutanoate hydroxymethyltransferase | Mycobacterium tuberculosis | Single protein | Chaudhuri, B N. | Kim, C Y. | Park, M S. | Sawaya, M R. | TBSGC, TB Structural Genomics Consortium. | Terwilliger, T C. | Waldo, G S. | Yeates, T O. | Domain swapping | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc