5dds

Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with PLP

spinqualitylabelsall models 5dds, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dds is a 4 chain structure with sequence from Actinoalloteichus sp. WH1-2216-6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: ACY, GOL, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H8Y6N2_9PSEU Publication Abstract from PubMed Caerulomycin A (CRM A 1) belongs to a family of natural products containing a 2,2'-bipyridyl ring core structure and is currently under development as a potent novel immunosuppressive agent. Herein, we report the functional characterization, kinetic analysis, substrate specificity, and structure insights of an aminotransferase CrmG in 1 biosynthesis. The aminotransferase CrmG was confirmed to catalyze a key transamination reaction to convert an aldehyde group to an amino group in the 1 biosynthetic pathway, preferring l-glutamate and l-glutamine as the amino donor substrates. The crystal structures of CrmG in complex with the cofactor 5'-pyridoxal phosphate (PLP) or 5'-pyridoxamine phosphate (PMP) or the acceptor substrate were determined to adopt a canonical fold-type I of PLP-dependent enzymes with a unique small additional domain. The structure guided site-directed mutagenesis identified key amino acid residues for substrate binding and catalytic activities, thus providing insights into the transamination mechanism of CrmG. Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis.,Zhu Y, Xu J, Mei X, Feng Z, Zhang L, Zhang Q, Zhang G, Zhu W, Liu J, Zhang C ACS Chem Biol. 2016 Apr 15;11(4):943-52. doi: 10.1021/acschembio.5b00984. Epub, 2016 Jan 12. PMID:26714051 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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