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1oy0
From Proteopedia
| 1oy0, resolution 2.80Å () | |||||||||
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| Ligands: | |||||||||
| Gene: | PANB (Mycobacterium tuberculosis) | ||||||||
| Activity: | 3-methyl-2-oxobutanoate hydroxymethyltransferase, with EC number 2.1.2.11 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1oy0 is a 5 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
- Chaudhuri BN, Sawaya MR, Kim CY, Waldo GS, Park MS, Terwilliger TC, Yeates TO. The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis. Structure. 2003 Jul;11(7):753-64. PMID:12842039
Categories: 3-methyl-2-oxobutanoate hydroxymethyltransferase | Mycobacterium tuberculosis | 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 | Transferase
