4hkg

Crystal Structure of Free-Standing Peptidyl Carrier Protein from Uncharacterized Acinetobacter baumannii Secondary Metabolic Pathway

spinqualitylabelsall models 4hkg, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hkg is a 2 chain structure with sequence from Acinetobacter baumannii AB307-0294. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3002Å Ligands: EDO, MRD, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Microorganisms produce a variety of natural products via secondary metabolic biosynthetic pathways. Two of these types of synthetic systems, the nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs), use large modular enzymes containing multiple catalytic domains in a single protein. These multidomain enzymes use an integrated carrier protein domain to transport the growing, covalently bound natural product to the neighboring catalytic domains for each step in the synthesis. Interestingly, some PKS and NRPS clusters contain free-standing domains that interact intermolecularly with other proteins. Being expressed outside the architecture of a multi-domain protein, these so-called type II proteins present challenges to understand the precise role they play. Additional structures of individual and multi-domain components of the NRPS enzymes will therefore provide a better understanding of the features that govern the domain interactions in these interesting enzyme systems. The high-resolution crystal structure of a free-standing carrier protein from Acinetobacter baumannii that belongs to a larger NRPS-containing operon, encoded by the ABBFA_003406-ABBFA_003399 genes of A. baumannii strain AB307-0294, that has been implicated in A. baumannii motility, quorum sensing and biofilm formation, is presented here. Comparison with the closest structural homologs of other carrier proteins identifies the requirements for a conserved glycine residue and additional important sequence and structural requirements within the regions that interact with partner proteins. Structural and bioinformatic characterization of an Acinetobacter baumannii type II carrier protein.,Allen CL, Gulick AM Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1718-25. doi:, 10.1107/S1399004714008311. Epub 2014 May 30. PMID:24914982 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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