6mni: Difference between revisions

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<StructureSection load='6mni' size='340' side='right'caption='[[6mni]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6mni' size='340' side='right'caption='[[6mni]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6mni]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MNI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MNI FirstGlance]. <br>
<table><tr><td colspan='2'>[[6mni]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cfbp_4909 Cfbp 4909]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MNI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mni OCA], [http://pdbe.org/6mni PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mni RCSB], [http://www.ebi.ac.uk/pdbsum/6mni PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mni ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KPSA3_03559 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103796 CFBP 4909])</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=6mni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mni OCA], [https://pdbe.org/6mni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mni RCSB], [https://www.ebi.ac.uk/pdbsum/6mni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mni ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chemotaxis is the process of sensing chemical gradients and navigating towards favourable conditions. Bacterial chemotaxis is mediated by arrays of trans-membrane chemoreceptor proteins. The most common class of chemoreceptors have periplasmic ligand-binding domains (LBDs) that detect extracellular chemical signs and transduce these signals to the downstream chemotaxis machinery. The repertoire of chemoreceptor proteins in a bacterium determines the range of environmental signals to which it can respond. Pseudomonas syringae pv. actinidiae (Psa) is a plant pathogen which causes bacterial canker of kiwifruit (Actinidia sp.). Compared to many other bacteria, Psa has a large number of chemoreceptors encoded in its genome (43) and most of these remain uncharacterized. A previous study identified PscC as a potential chemoreceptor for l-proline and other amino acid ligands. Here, we have characterized the interaction of PscC-LBD with l-proline using a combination of isothermal titration calorimetry (ITC) and X-ray crystallography. ITC confirmed direct binding of l-proline to PscC-LBD with KD value of 5.0 muM. We determined the structure of PscC-LBD in complex with l-proline. Our structural analysis showed that PscC-LBD adopts similar double-CACHE fold to several other amino acid chemoreceptors. A comparison of the PscC-LDB to other dCACHE structures highlights residues in the binding cavity which contribute to its ligand specificity.
Structure of a double CACHE chemoreceptor ligand-binding domain from Pseudomonas syringae provides insights into the basis of proline recognition.,Ehrhardt MKG, Gerth ML, Johnston JM Biochem Biophys Res Commun. 2021 Apr 16;549:194-199. doi:, 10.1016/j.bbrc.2021.02.090. Epub 2021 Mar 12. PMID:33721671<ref>PMID:33721671</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6mni" style="background-color:#fffaf0;"></div>
==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cfbp 4909]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ehrhardt, M K.G]]
[[Category: Ehrhardt, M K.G]]