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< | ==The Structure Of A DnaB-Like Replicative Helicase And Its Interactions With Primase== | ||
<StructureSection load='3bgw' size='340' side='right'caption='[[3bgw]], [[Resolution|resolution]] 3.91Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bgw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_SPP1 Bacillus phage SPP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BGW 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]] 3.91Å</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=3bgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bgw OCA], [https://pdbe.org/3bgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bgw RCSB], [https://www.ebi.ac.uk/pdbsum/3bgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bgw ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q38152_BPSPP Q38152_BPSPP] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/3bgw_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bgw ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Helicases are essential enzymes for DNA replication, a fundamental process in all living organisms. The DnaB family are hexameric replicative helicases that unwind duplex DNA and coordinate with RNA primase and other proteins at the replication fork in prokaryotes. Here, we report the full-length crystal structure of G40P, a DnaB family helicase. The hexamer complex reveals an unusual architectural feature and a new type of assembly mechanism. The hexamer has two tiers: a three-fold symmetric N-terminal tier and a six-fold symmetric C-terminal tier. Monomers with two different conformations, termed cis and trans, come together to provide a topological solution for the dual symmetry within a hexamer. Structure-guided mutational studies indicate an important role for the N-terminal tier in binding primase and regulating primase-mediated stimulation of helicase activity. This study provides insights into the structural and functional interplay between G40P helicase and DnaG primase. | |||
The structure of a DnaB-family replicative helicase and its interactions with primase.,Wang G, Klein MG, Tokonzaba E, Zhang Y, Holden LG, Chen XS Nat Struct Mol Biol. 2008 Jan;15(1):94-100. Epub 2007 Dec 23. PMID:18157148<ref>PMID:18157148</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3bgw" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Bacillus phage SPP1]] | ||
[[Category: Large Structures]] | |||
[[Category: Chen XS]] | |||
== | [[Category: Holden LG]] | ||
[[Category: Klein MG]] | |||
[[Category: Bacillus phage | [[Category: Tokonzaba E]] | ||
[[Category: | [[Category: Wang G]] | ||
[[Category: Chen | [[Category: Zhang Y]] | ||
[[Category: Holden | |||
[[Category: Klein | |||
[[Category: Tokonzaba | |||
[[Category: Wang | |||
[[Category: Zhang | |||
Latest revision as of 10:53, 9 October 2024
The Structure Of A DnaB-Like Replicative Helicase And Its Interactions With PrimaseThe Structure Of A DnaB-Like Replicative Helicase And Its Interactions With Primase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHelicases are essential enzymes for DNA replication, a fundamental process in all living organisms. The DnaB family are hexameric replicative helicases that unwind duplex DNA and coordinate with RNA primase and other proteins at the replication fork in prokaryotes. Here, we report the full-length crystal structure of G40P, a DnaB family helicase. The hexamer complex reveals an unusual architectural feature and a new type of assembly mechanism. The hexamer has two tiers: a three-fold symmetric N-terminal tier and a six-fold symmetric C-terminal tier. Monomers with two different conformations, termed cis and trans, come together to provide a topological solution for the dual symmetry within a hexamer. Structure-guided mutational studies indicate an important role for the N-terminal tier in binding primase and regulating primase-mediated stimulation of helicase activity. This study provides insights into the structural and functional interplay between G40P helicase and DnaG primase. The structure of a DnaB-family replicative helicase and its interactions with primase.,Wang G, Klein MG, Tokonzaba E, Zhang Y, Holden LG, Chen XS Nat Struct Mol Biol. 2008 Jan;15(1):94-100. Epub 2007 Dec 23. PMID:18157148[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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