4QBU
Structure of the Acyl Transferase domain of ZmaA
Summary for 4QBU
| Entry DOI | 10.2210/pdb4qbu/pdb |
| Descriptor | ZmaA, FORMIC ACID (3 entities in total) |
| Functional Keywords | acyl transferase, polyketide synthase, acyl carrier protein, transferase |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 1 |
| Total formula weight | 50904.90 |
| Authors | Dyer, D.H.,Kevany, B.M.,Thomas, M.G.,Forest, K.T. (deposition date: 2014-05-08, release date: 2014-11-05, Last modification date: 2023-09-20) |
| Primary citation | Park, H.,Kevany, B.M.,Dyer, D.H.,Thomas, M.G.,Forest, K.T. A Polyketide Synthase Acyltransferase Domain Structure Suggests a Recognition Mechanism for Its Hydroxymalonyl-Acyl Carrier Protein Substrate. Plos One, 9:e110965-e110965, 2014 Cited by PubMed Abstract: We have previously shown that the acyl transferase domain of ZmaA (ZmaA-AT) is involved in the biosynthesis of the aminopolyol polyketide/nonribosomal peptide hybrid molecule zwittermicin A from cereus UW85, and that it specifically recognizes the precursor hydroxymalonyl-acyl carrier protein (ACP) and transfers the hydroxymalonyl extender unit to a downstream second ACP via a transacylated AT domain intermediate. We now present the X-ray crystal structure of ZmaA-AT at a resolution of 1.7 Å. The structure shows a patch of solvent-exposed hydrophobic residues in the area where the AT is proposed to interact with the precursor ACP. We addressed the significance of the AT/ACP interaction in precursor specificity of the AT by testing whether malonyl- or methylmalonyl-ACP can be recognized by ZmaA-AT. We found that the ACP itself biases extender unit selection. Until now, structural information for ATs has been limited to ATs specific for the CoA-linked precursors malonyl-CoA and (2S)-methylmalonyl-CoA. This work contributes to polyketide synthase engineering efforts by expanding our knowledge of AT/substrate interactions with the structure of an AT domain that recognizes an ACP-linked substrate, the rare hydroxymalonate. Our structure suggests a model in which ACP interaction with a hydrophobic motif promotes secondary structure formation at the binding site, and opening of the adjacent substrate pocket lid to allow extender unit binding in the AT active site. PubMed: 25340352DOI: 10.1371/journal.pone.0110965 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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