3CYP
The crystal structure of the C-terminal domain of Helicobacter pylori MotB (residues 125-256).
Summary for 3CYP
| Entry DOI | 10.2210/pdb3cyp/pdb |
| Related | 3CYQ |
| Descriptor | Chemotaxis protein motB (2 entities in total) |
| Functional Keywords | helicobacter pylori, bacterial flagellar motor, peptidoglycan binding, bacterial flagellum, chemotaxis, flagellar rotation, inner membrane, membrane, transmembrane, membrane protein |
| 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 | 4 |
| Total formula weight | 63759.94 |
| Authors | Roujeinikova, A. (deposition date: 2008-04-26, release date: 2008-07-08, Last modification date: 2024-02-21) |
| Primary citation | Roujeinikova, A. Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: implications for peptidoglycan recognition. Proc.Natl.Acad.Sci.Usa, 105:10348-10353, 2008 Cited by PubMed Abstract: The stator ring of the bacterial flagellar motor is composed of the MotA and MotB proteins that act together to generate a turning force (torque) acting on the FliG ring of the rotor. The C-terminal domain of MotB (MotB-C) is believed to anchor the MotA/MotB complex to peptidoglycan (PG) of the cell wall. The first crystal structures of MotB-C and its complex with N-acetylmuramic acid (NAM) have been determined to 1.6- and 2.3-A resolution, respectively. MotB-C is a dimer, both in solution and in the crystal. The two glycan chains of the PG ligand can be modeled as semirigid helices and docked into the grooves harboring the NAM molecules on the opposite faces of the dimer. The model suggests that a concave hydrophilic surface created upon edge-to-edge beta-sheet dimerization and centered around the 2-fold axis of the dimer can accommodate the peptide cross-bridge linking the two sugar chains. Significant structural similarities were found between MotB-C and the PG-binding domains of reduction-modifiable protein M and peptidoglycan-associated lipoprotein exclude, suggesting that PG recognition by different outer membrane protein A-like proteins may be governed by very similar molecular mechanisms that evidently involve protein dimerization. PubMed: 18647830DOI: 10.1073/pnas.0803039105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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