2qo3
From Proteopedia
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Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase
Overview
We report the 2.6 A X-ray crystal structure of a 190 kDa homodimeric, fragment from module 3 of the 6-deoxyerthronolide B synthase covalently, bound to the inhibitor cerulenin. The structure shows two well-organized, interdomain linker regions in addition to the full-length ketosynthase, (KS) and acyltransferase (AT) domains. Analysis of the substrate-binding, site of the KS domain suggests that a loop region at the homodimer, interface influences KS substrate specificity. We also describe a model, for the interaction of the catalytic domains with the acyl carrier protein, (ACP) domain. The ACP is proposed to dock within a deep cleft between the, KS and AT domains, with interactions that span both the KS homodimer and, AT domain. In conjunction with other recent data, our results provide, atomic resolution pictures of several catalytically relevant protein, interactions in this remarkable family of modular megasynthases.
About this Structure
2QO3 is a Single protein structure of sequence from Saccharopolyspora erythraea with ACT, CL and CER as ligands. Active as Erythronolide synthase, with EC number 2.3.1.94 Full crystallographic information is available from OCA.
Reference
Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase., Tang Y, Chen AY, Kim CY, Cane DE, Khosla C, Chem Biol. 2007 Aug;14(8):931-43. PMID:17719492
Page seeded by OCA on Wed Nov 21 13:52:17 2007
