2QO3

Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase

Summary for 2QO3

• Entry DOI: 10.2210/pdb2qo3/pdb
• Related: 2HG4
• Descriptor: EryAII Erythromycin polyketide synthase modules 3 and 4, ACETATE ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: ketosynthase, acyltransferase, phosphopantetheine, transferase
• Biological source: Saccharopolyspora erythraea
• Total number of polymer chains: 2
• Total formula weight: 194017.92

Authors

Khosla, C.,Cane, E.D.,Tang, Y.,Chen, Y.A.,Kim, C.Y. (deposition date: 2007-07-19, release date: 2007-09-04, Last modification date: 2024-11-06)

Primary citation

Tang, Y.,Chen, Y.A.,Kim, C.Y.,Cane, E.D.,Khosla, C.
Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase
Chem.Biol., 14:931-943, 2007

PubMed Abstract: 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.

PubMed: 17719492
DOI: 10.1016/j.chembiol.2007.07.012

Experimental method

X-RAY DIFFRACTION (2.59 Å)