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

Summary for 1OY0

• Entry DOI: 10.2210/pdb1oy0/pdb
• Descriptor: Ketopantoate hydroxymethyltransferase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: domain swapping, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cytoplasm (Potential): P0A5Q8
• Total number of polymer chains: 5
• Total formula weight: 146947.96

Authors

Chaudhuri, B.N.,Sawaya, M.R.,Kim, C.Y.,Waldo, G.S.,Park, M.S.,Terwilliger, T.C.,Yeates, T.O.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2003-04-03, release date: 2003-07-15, Last modification date: 2024-02-14)

Primary citation

Chaudhuri, B.N.,Sawaya, M.R.,Kim, C.Y.,Waldo, G.S.,Park, M.S.,Terwilliger, T.C.,Yeates, T.O.
The Crystal Structure of the First Enzyme in the Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase, from M. tuberculosis
Structure, 11:753-764, 2003

PubMed Abstract: 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.

PubMed: 12842039
DOI: 10.1016/S0969-2126(03)00106-0

Experimental method

X-RAY DIFFRACTION (2.8 Å)