7qxm: Difference between revisions
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The | ==Crystal structure of the Vibrio cholerae replicative helicase (DnaB)== | ||
<StructureSection load='7qxm' size='340' side='right'caption='[[7qxm]], [[Resolution|resolution]] 3.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7qxm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QXM 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]] 3.8Å</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=7qxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qxm OCA], [https://pdbe.org/7qxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qxm RCSB], [https://www.ebi.ac.uk/pdbsum/7qxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qxm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A085R2T8_VIBCL A0A085R2T8_VIBCL] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.[ARBA:ARBA00003574][RuleBase:RU362085] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To enable chromosomal replication, DNA is unwound by the ATPase molecular motor replicative helicase. The bacterial helicase DnaB is a ring-shaped homo-hexamer whose conformational dynamics are being studied through its different 3D structural states adopted along its functional cycle. Our findings describe a new crystal structure for the apo-DnaB from Vibrio cholerae, forming a planar hexamer with pseudo-symmetry, constituted by a trimer of dimers in which the C-terminal domains delimit a triskelion-shaped hole. This hexamer is labile and inactive. We suggest that it represents an intermediate state allowing the formation of the active NTP-bound hexamer from dimers. | |||
The apo-form of the Vibrio cholerae replicative helicase DnaB is a labile and inactive planar trimer of dimers.,Cargemel C, Walbott H, Durand D, Legrand P, Ouldali M, Ferat JL, Marsin S, Quevillon-Cheruel S FEBS Lett. 2022 May 14. doi: 10.1002/1873-3468.14403. PMID:35568982<ref>PMID:35568982</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7qxm" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Vibrio cholerae]] | |||
[[Category: Cargemel C]] | |||
[[Category: Legrand P]] | |||
[[Category: Quevillon-Cheruel S]] | |||
[[Category: Walbott H]] |
Latest revision as of 16:23, 1 February 2024
Crystal structure of the Vibrio cholerae replicative helicase (DnaB)Crystal structure of the Vibrio cholerae replicative helicase (DnaB)
Structural highlights
FunctionA0A085R2T8_VIBCL Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.[ARBA:ARBA00003574][RuleBase:RU362085] Publication Abstract from PubMedTo enable chromosomal replication, DNA is unwound by the ATPase molecular motor replicative helicase. The bacterial helicase DnaB is a ring-shaped homo-hexamer whose conformational dynamics are being studied through its different 3D structural states adopted along its functional cycle. Our findings describe a new crystal structure for the apo-DnaB from Vibrio cholerae, forming a planar hexamer with pseudo-symmetry, constituted by a trimer of dimers in which the C-terminal domains delimit a triskelion-shaped hole. This hexamer is labile and inactive. We suggest that it represents an intermediate state allowing the formation of the active NTP-bound hexamer from dimers. The apo-form of the Vibrio cholerae replicative helicase DnaB is a labile and inactive planar trimer of dimers.,Cargemel C, Walbott H, Durand D, Legrand P, Ouldali M, Ferat JL, Marsin S, Quevillon-Cheruel S FEBS Lett. 2022 May 14. doi: 10.1002/1873-3468.14403. PMID:35568982[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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