1m3u

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{{STRUCTURE_1m3u| PDB=1m3u | SCENE= }}
{{STRUCTURE_1m3u| PDB=1m3u | SCENE= }}
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'''Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate'''
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===Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate===
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==Overview==
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We report the crystal structure of E. coli ketopantoate hydroxymethyltransferase (KPHMT) at 1.9 A resolution, in complex with its product, ketopantoate. KPHMT catalyzes the first step in the biosynthesis of pantothenate (vitamin B(5)), the precursor of coenzyme A and the acyl carrier protein cofactor. The structure of the decameric enzyme was solved by multiwavelength anomalous dispersion to locate 160 selenomethionine sites and phase 560 kDa of protein, making it the largest structure solved by this approach. KPHMT adopts the (betaalpha)(8) barrel fold and is a member of the phosphoenolpyruvate/pyruvate superfamily. The active site contains a ketopantoate bidentately coordinated to Mg(2+). Similar binding is likely for the substrate, alpha-ketoisovalerate, orienting the C3 for deprotonation.
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==About this Structure==
==About this Structure==
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[[Category: Selenomethionine mad]]
[[Category: Selenomethionine mad]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
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Revision as of 20:08, 2 July 2008

Image:1m3u.png

Template:STRUCTURE 1m3u

Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate

Template:ABSTRACT PUBMED 12906829

About this Structure

1M3U is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites., von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C, Structure. 2003 Aug;11(8):985-96. PMID:12906829

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