3IMP

New crystal form of the C-terminal domain of Helicobacter pylori MotB (residues 125-256)

Summary for 3IMP

• Entry DOI: 10.2210/pdb3imp/pdb
• Related: 3CYP 3CYQ
• Descriptor: Chemotaxis protein motB, NICKEL (II) ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: peptidoglycan binding, bacterial flagellum, chemotaxis, flagellar rotation, inner membrane, membrane, transmembrane, membrane protein, cell inner membrane, cell membrane
• Biological source: Helicobacter pylori (Campylobacter pylori)
• Cellular location: Cell inner membrane (By similarity); Single- pass type II membrane protein (Potential): P56427
• Total number of polymer chains: 12
• Total formula weight: 191539.01

Authors

Roujeinikova, A. (deposition date: 2009-08-11, release date: 2010-08-04, Last modification date: 2023-11-01)

Primary citation

Reboul, C.F.,Andrews, D.A.,Nahar, M.F.,Buckle, A.M.,Roujeinikova, A.
Crystallographic and Molecular Dynamics Analysis of Loop Motions Unmasking the Peptidoglycan-Binding Site in Stator Protein MotB of Flagellar Motor
Plos One, 6:e18981-e18981, 2011

PubMed Abstract: The C-terminal domain of MotB (MotB-C) shows high sequence similarity to outer membrane protein A and related peptidoglycan (PG)-binding proteins. It is believed to anchor the power-generating MotA/MotB stator unit of the bacterial flagellar motor to the peptidoglycan layer of the cell wall. We previously reported the first crystal structure of this domain and made a puzzling observation that all conserved residues that are thought to be essential for PG recognition are buried and inaccessible in the crystal structure. In this study, we tested a hypothesis that peptidoglycan binding is preceded by, or accompanied by, some structural reorganization that exposes the key conserved residues.

PubMed: 21533052
DOI: 10.1371/journal.pone.0018981

Experimental method

X-RAY DIFFRACTION (2.5 Å)