1MZJ

Crystal Structure of the Priming beta-Ketosynthase from the R1128 Polyketide Biosynthetic Pathway

Summary for 1MZJ

• Entry DOI: 10.2210/pdb1mzj/pdb
• Related: 1EBL
• Descriptor: Beta-ketoacylsynthase III, COENZYME A, ACETYL GROUP, ... (4 entities in total)
• Functional Keywords: beta-ketosynthase, aromatic polyketide, biosynthetic engineering, catalytic triad, transferase
• Biological source: Streptomyces sp. R1128
• Cellular location: Cytoplasm (Probable): Q9F6D4
• Total number of polymer chains: 2
• Total formula weight: 72479.26

Authors

Pan, H.,Tsai, S.C.,Meadows, E.S.,Miercke, L.J.W.,Keatinge-Clay, A.,O'Connell, J.,Khosla, C.,Stroud, R.M. (deposition date: 2002-10-08, release date: 2002-12-11, Last modification date: 2025-03-26)

Primary citation

Pan, H.,Tsai, S.,Meadows, E.S.,Miercke, L.J.,Keatinge-Clay, A.T.,O'Connell, J.,Khosla, C.,Stroud, R.M.
Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway
Structure, 10:1559-1568,

PubMed Abstract: 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.

PubMed: 12429097
DOI: 10.1016/S0969-2126(02)00889-4

Experimental method

X-RAY DIFFRACTION (2.1 Å)