7b22

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'''Unreleased structure'''
 
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The entry 7b22 is ON HOLD until Paper Publication
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==Vibrio cholerae ParD2 Antitoxin==
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<StructureSection load='7b22' size='340' side='right'caption='[[7b22]], [[Resolution|resolution]] 3.08&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7b22]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B22 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.08&#8491;</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=7b22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b22 OCA], [https://pdbe.org/7b22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b22 RCSB], [https://www.ebi.ac.uk/pdbsum/7b22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b22 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PARD_VIBCH PARD_VIBCH] Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the effect of toxin ParE (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ParD2 is the antitoxin component of the parDE2 toxin-antitoxin module from Vibrio cholerae and consists of an ordered DNA-binding domain followed by an intrinsically disordered ParE-neutralizing domain. In the absence of the C-terminal intrinsically disordered protein (IDP) domain, V. cholerae ParD2 (VcParD2) crystallizes as a doughnut-shaped hexadecamer formed by the association of eight dimers. This assembly is stabilized via hydrogen bonds and salt bridges rather than by hydrophobic contacts. In solution, oligomerization of the full-length protein is restricted to a stable, open decamer or dodecamer, which is likely to be a consequence of entropic pressure from the IDP tails. The relative positioning of successive VcParD2 dimers mimics the arrangement of Streptococcus agalactiae CopG dimers on their operator and allows an extended operator to wrap around the VcParD2 oligomer.
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Authors: Garcia-Rodriguez, G., Loris, R.
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Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.,Garcia-Rodriguez G, Girardin Y, Volkov AN, Singh RK, Muruganandam G, Van Dyck J, Sobott F, Versees W, Charlier D, Loris R Acta Crystallogr D Struct Biol. 2021 Jul 1;77(Pt 7):904-920. doi:, 10.1107/S2059798321004873. Epub 2021 Jun 18. PMID:34196617<ref>PMID:34196617</ref>
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Description: Vibrio cholerae ParD2 Antitoxin
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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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[[Category: Garcia-Rodriguez, G]]
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<div class="pdbe-citations 7b22" style="background-color:#fffaf0;"></div>
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[[Category: Loris, R]]
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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: Vibrio cholerae O1 biovar El Tor str. N16961]]
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[[Category: Garcia-Rodriguez G]]
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[[Category: Loris R]]

Current revision

Vibrio cholerae ParD2 Antitoxin

PDB ID 7b22

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