2hg4

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spinqualitylabelsall models PDB ID 2hg4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.73Å
Ligands:	, and
Gene:	eryA (Saccharopolyspora erythraea)
Activity:	Erythronolide synthase, with EC number 2.3.1.94
Coordinates:	save as pdb, mmCIF, xml

Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.

Overview

The x-ray crystal structure of a 194-kDa fragment from module 5 of the 6-deoxyerythronolide B synthase has been solved at 2.7 Angstrom resolution. Each subunit of the homodimeric protein contains a full-length ketosynthase (KS) and acyl transferase (AT) domain as well as three flanking "linkers." The linkers are structurally well defined and contribute extensively to intersubunit or interdomain interactions, frequently by means of multiple highly conserved residues. The crystal structure also reveals that the active site residue Cys-199 of the KS domain is separated from the active site residue Ser-642 of the AT domain by approximately 80 Angstrom. This distance is too large to be covered simply by alternative positioning of a statically anchored, fully extended phosphopantetheine arm of the acyl carrier protein domain from module 5. Thus, substantial domain reorganization appears necessary for the acyl carrier protein to interact successively with both the AT and the KS domains of this prototypical polyketide synthase module. The 2.7-Angstrom KS-AT structure is fully consistent with a recently reported lower resolution, 4.5-Angstrom model of fatty acid synthase structure, and emphasizes the close biochemical and structural similarity between polyketide synthase and fatty acid synthase enzymology.

About this Structure

2HG4 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

Reference

The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase., Tang Y, Kim CY, Mathews II, Cane DE, Khosla C, Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11124-9. Epub 2006 Jul 14. PMID:16844787

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