1mzj
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(New page: 200px<br /><applet load="1mzj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mzj, resolution 2.1Å" /> '''Crystal Structure of ...)
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Revision as of 19:42, 20 November 2007
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Crystal Structure of the Priming beta-Ketosynthase from the R1128 Polyketide Biosynthetic Pathway
Overview
ZhuH is a priming ketosynthase that initiates the elongation of the, polyketide chain in the biosynthetic pathway of a type II polyketide, R1128. The crystal structure of ZhuH in complex with the priming substrate, acetyl-CoA reveals an extensive loop region at the dimer interface that, appears to affect the selectivity for the primer unit. Acetyl-CoA is bound, in a 20 A-long channel, which placed the acetyl group against the, catalytic triad. Analysis of the primer unit binding site in ZhuH suggests, that it can accommodate acyl chains that are two to four carbons long., Selectivity and primer unit size appear to involve the side chains of, three residues on the loops close to the dimer interface that constitute, the bottom of the substrate binding pocket.
About this Structure
1MZJ is a Single protein structure of sequence from Streptomyces sp. r22 with COA and ACE as ligands. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway., Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM, Structure. 2002 Nov;10(11):1559-68. PMID:12429097
Page seeded by OCA on Tue Nov 20 21:49:52 2007
Categories: Beta-ketoacyl-acyl-carrier-protein synthase I | Single protein | Streptomyces sp. r22 | Connell, J.O. | Keatinge-Clay, A. | Khosla, C. | Meadows, E.S. | Miercke, L.J.W. | Pan, H. | Stroud, R.M. | Tsai, S.C. | ACE | COA | Aromatic polyketide | Beta-ketosynthase | Biosynthetic engineering | Catalytic triad