View source for 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)==
<StructureSection load='6pzj' size='340' side='right'caption='[[6pzj]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pzj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_interrogans_serovar_Copenhageni_str._Fiocruz_L1-130 Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PZJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pzj OCA], [https://pdbe.org/6pzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pzj RCSB], [https://www.ebi.ac.uk/pdbsum/6pzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pzj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q72NB4_LEPIC Q72NB4_LEPIC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 alpha/beta 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.

Structural analysis of CACHE domain of the McpA chemoreceptor from Leptospira interrogans.,Santos JC, Vieira ML, Abendroth J, Lin T, Staker BL, Myler PJ, Nascimento ALTO Biochem Biophys Res Commun. 2020 Dec 17;533(4):1323-1329. doi: , 10.1016/j.bbrc.2020.10.013. Epub 2020 Oct 21. PMID:33097187<ref>PMID:33097187</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pzj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130]]