3euq

X-ray structural of a type III pentaketide synthase from Neurospora crassa

spinqualitylabelsall models 3euq, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3euq is a 4 chain structure with sequence from Neurospora crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CSD, P6G Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7S6N4_NEUCR Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The fungal type III polyketide synthase 2'-oxoalkylresorcylic acid synthase (ORAS) primes with a range of acyl-Coenzyme A thioesters (C4-C20) and extends using malonyl-Coenzyme A to produce pyrones, resorcinols, and resorcylic acids. To gain insight into this unusual substrate specificity and product profile, we have determined the crystal structures of ORAS to 1.75 A resolution, the Phe-252-->Gly site-directed mutant to 2.1 A resolution, and a binary complex of ORAS with eicosanoic acid to 2.0 A resolution. The structures reveal a distinct rearrangement of structural elements near the active site that allows accommodation of long-chain fatty acid esters and a reorientation of the gating mechanism that controls cyclization and polyketide chain length. The roles of these structural elements are further elucidated by characterization of various structure-based site-directed variants. These studies establish an unexpected plasticity to the PKS fold, unanticipated from structural studies of other members of this enzyme family. Distinct structural elements dictate the specificity of the type III pentaketide synthase from Neurospora crassa.,Rubin-Pitel SB, Zhang H, Vu T, Brunzelle JS, Zhao H, Nair SK Chem Biol. 2008 Oct 20;15(10):1079-90. PMID:18940668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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