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1z8s
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1z8s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z8s" /> '''DnaB binding domain of DnaG (P16) from Bacil...) |
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| - | [[Image:1z8s.gif|left|200px]]<br /><applet load="1z8s" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1z8s" /> | ||
| - | '''DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)'''<br /> | ||
| - | == | + | ==DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)== |
| - | The helicase-primase interaction is a critical event in DNA replication | + | <StructureSection load='1z8s' size='340' side='right'caption='[[1z8s]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1z8s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z8S FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1z8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z8s OCA], [https://pdbe.org/1z8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z8s RCSB], [https://www.ebi.ac.uk/pdbsum/1z8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z8s ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DNAG_GEOSE DNAG_GEOSE] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974] | ||
| + | == 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/z8/1z8s_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1z8s ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The helicase-primase interaction is a critical event in DNA replication and is mediated by a putative helicase-interaction domain within the primase. The solution structure of the helicase-interaction domain of DnaG reveals that it is made up of two independent subdomains: an N-terminal six-helix module and a C-terminal two-helix module that contains the residues of the primase previously identified as important in the interaction with the helicase. We show that the two-helix module alone is sufficient for strong binding between the primase and the helicase but fails to activate the helicase; both subdomains are required for helicase activation. The six-helix module of the primase has only one close structural homolog, the N-terminal domain of the corresponding helicase. This surprising structural relationship, coupled with the differences in surface properties of the two molecules, suggests how the helicase-interaction domain may perturb the structure of the helicase and lead to activation. | ||
| - | + | Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.,Syson K, Thirlway J, Hounslow AM, Soultanas P, Waltho JP Structure. 2005 Apr;13(4):609-16. PMID:15837199<ref>PMID:15837199</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1z8s" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Geobacillus stearothermophilus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hounslow AM]] | ||
| + | [[Category: Soultanas P]] | ||
| + | [[Category: Syson K]] | ||
| + | [[Category: Thirlway J]] | ||
| + | [[Category: Waltho JP]] | ||
Current revision
DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)
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