6g5s

Solution structure of the TPR domain of the cell division coordinator, CpoB

spinqualitylabelsall models 6g5s Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6g5s is a 1 chain structure with sequence from Escherichia coli K-12. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CPOB_ECOLI Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division. Promotes physical and functional coordination of the PBP1B-LpoB and Tol machines, and regulates PBP1B activity in response to Tol energy state. Publication Abstract from PubMed Bacteria surround their cytoplasmic membrane with an essential, stress-bearing peptidoglycan (PG) layer consisting of glycan chains linked by short peptides into a mesh-like structure. Growing and dividing cells expand their PG layer using inner-membrane anchored PG synthases, including Penicillin-binding proteins (PBPs), which participate in dynamic protein complexes to facilitate cell wall growth. In Escherichia coli, and presumably other Gram-negative bacteria, growth of the mainly single layered PG is regulated by outer membrane-anchored lipoproteins. The lipoprotein LpoB is required to activate PBP1B, which is a major, bi-functional PG synthase with glycan chain polymerizing (glycosyltransferase) and peptide cross-linking (transpeptidase) activities. In this work we show how the binding of LpoB to the regulatory UB2H domain of PBP1B activates both activities. Binding induces structural changes in the UB2H domain, which transduce to the two catalytic domains by distinct allosteric pathways. We also show how an additional regulator protein, CpoB, is able to selectively modulate the TPase activation by LpoB without interfering with GTase activation. This article is protected by copyright. All rights reserved. Induced conformational changes activate the peptidoglycan synthase PBP1B.,Egan AJF, Maya-Martinez R, Ayala I, Bougault CM, Banzhaf M, Breukink E, Vollmer W, Simorre JP Mol Microbiol. 2018 Jul 25. doi: 10.1111/mmi.14082. PMID:30044025 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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