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4HKG

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

Summary for 4HKG
Entry DOI10.2210/pdb4hkg/pdb
DescriptorPhosphopantetheine attachment site family protein, (4R)-2-METHYLPENTANE-2,4-DIOL, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsnrps, non-ribosomal peptide synthetase, peptidyl carrier protein, phosphopantetheine attachment site, phosphopantetheine binding protein
Biological sourceAcinetobacter baumannii
Total number of polymer chains2
Total formula weight20106.71
Authors
Allen, C.L.,Gulick, A.M. (deposition date: 2012-10-15, release date: 2013-10-30, Last modification date: 2023-09-20)
Primary citationAllen, C.L.,Gulick, A.M.
Structural and bioinformatic characterization of an Acinetobacter baumannii type II carrier protein.
Acta Crystallogr. D Biol. Crystallogr., 70:1718-1725, 2014
Cited by
PubMed Abstract: 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.
PubMed: 24914982
DOI: 10.1107/S1399004714008311
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3002 Å)
Structure validation

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