6zz9

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(New page: '''Unreleased structure''' The entry 6zz9 is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (06:09, 2 March 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6zz9 is ON HOLD
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==Crystal structure of CbpB from Streptococcus agalactiae==
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<StructureSection load='6zz9' size='340' side='right'caption='[[6zz9]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6zz9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZZ9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6zz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zz9 OCA], [https://pdbe.org/6zz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zz9 RCSB], [https://www.ebi.ac.uk/pdbsum/6zz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zz9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A076YWK5_STRAG A0A076YWK5_STRAG]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclic di-AMP is an essential signalling molecule in Gram-positive bacteria. This second messenger regulates the osmotic pressure of the cell by interacting directly with the regulatory domains, either RCK_C or CBS domains, of several potassium and osmolyte uptake membrane protein systems. Cyclic di-AMP also targets stand-alone CBS domain proteins such as DarB in Bacillus subtilis and CbpB in Listeria monocytogenes. We show here that the CbpB protein of Group B Streptococcus binds c-di-AMP with a very high affinity. Crystal structures of CbpB reveal the determinants of binding specificity and significant conformational changes occurring upon c-di-AMP binding. Deletion of the cbpB gene alters bacterial growth in low potassium conditions most likely due to a decrease in the amount of ppGpp caused by a loss of interaction between CbpB and Rel, the GTP/GDP pyrophosphokinase.
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Authors:
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The c-di-AMP-binding protein CbpB modulates the level of ppGpp alarmone in Streptococcus agalactiae.,Covaleda-Cortes G, Mechaly A, Brissac T, Baehre H, Devaux L, England P, Raynal B, Hoos S, Gominet M, Firon A, Trieu-Cuot P, Kaminski PA FEBS J. 2023 Jan 11. doi: 10.1111/febs.16724. PMID:36629470<ref>PMID:36629470</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6zz9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptococcus agalactiae]]
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[[Category: Covaleda-Cortes G]]
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[[Category: Kaminski PA]]
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[[Category: Mechaly AE]]

Current revision

Crystal structure of CbpB from Streptococcus agalactiae

PDB ID 6zz9

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