2vsq | pdb_00002vsq

STRUCTURE OF SURFACTIN A SYNTHETASE C (SRFA-C), A NONRIBOSOMAL PEPTIDE SYNTHETASE TERMINATION MODULE

spinqualitylabelsall models 2vsq, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vsq is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. Ligands: LEU, SO4 Related: 1jmk Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum 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 Nonribosomal peptide synthetases (NRPS) are modularly organized megaenzymes that act as an assembly line to catalyze the biosynthesis of complex natural products. The crystal structure of the 144 kD termination module SrfA-C that comprises four essential domains was solved at 2.6 A resolution. Its architecture shows that the adenylation and condensation domains associate closely to form a catalytic platform with their active sites on the same side of the platform. The peptidyl-carrier domain is flexibly tethered to this platform and thus able to move with its substrate-loaded 4-phosphopantetheine arm between the active site of the adenylation domain and the donor side of the condensation domain. Furthermore, the SrfA-C crystal structure inspires further investigations on rational redesign of NRPS for production of novel bioactive peptides. Crystal Structure of the Termination Module of a Nonribosomal Peptide Synthetase.,Tanovic A, Samel SA, Essen LO, Marahiel MA Science. 2008 Jun 26;. PMID:18583577 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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