6PZJ
Structure of the N-terminal domain (residues 43-304) of Methyl-accepting chemotaxis protein from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Copenhageni (strain Fiocruz L1-130)
Summary for 6PZJ
| Entry DOI | 10.2210/pdb6pzj/pdb |
| Descriptor | Methyl-accepting chemotaxis protein, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | ssgcid, structural genomics, seattle structural genomics center for infectious disease, signaling protein |
| Biological source | Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) |
| Total number of polymer chains | 1 |
| Total formula weight | 31829.32 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2019-07-31, release date: 2019-08-14, Last modification date: 2024-08-07) |
| Primary citation | Santos, J.C.,Vieira, M.L.,Abendroth, J.,Lin, T.,Staker, B.L.,Myler, P.J.,Nascimento, A.L.T.O. Structural analysis of CACHE domain of the McpA chemoreceptor from Leptospira interrogans. Biochem.Biophys.Res.Commun., 533:1323-1329, 2020 Cited by PubMed Abstract: Leptospira is a genus of spirochete bacteria highly motile that includes pathogenic species responsible to cause leptospirosis disease. Chemotaxis and motility are required for Leptospira infectivity, pathogenesis, and invasion of bacteria into the host. In prokaryotes, the most common chemoreceptors are methyl-accepting chemotaxis proteins that have a role play to detect the chemical signals and move to a favorable environment for its survival. Here, we report the first crystal structure of CACHE domain of the methyl-accepting chemotaxis protein (McpA) of L. interrogans. The structural analysis showed that McpA adopts similar α/β architecture of several other bacteria chemoreceptors. We also found a typical dimerization interface that appears to be functionally crucial for signal transmission and chemotaxis. In addition to McpA structural analyses, we have identified homologous proteins and conservative functional regions using bioinformatics techniques. These results improve our understanding the relationship between chemoreceptor structures and functions of Leptospira species. PubMed: 33097187DOI: 10.1016/j.bbrc.2020.10.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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