1oy0
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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OverviewOverview
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 StructureAbout this Structure
1OY0 is a Single protein structure of sequence from Mycobacterium tuberculosis with MG as ligand. Active as 3-methyl-2-oxobutanoate hydroxymethyltransferase, with EC number 2.1.2.11 Full crystallographic information is available from OCA.
ReferenceReference
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
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