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| | ==Crystal structure of C-terminal domain of Helicobacter pylori DnaB Helicase== | | ==Crystal structure of C-terminal domain of Helicobacter pylori DnaB Helicase== |
| - | <StructureSection load='4a1f' size='340' side='right' caption='[[4a1f]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4a1f' size='340' side='right'caption='[[4a1f]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a1f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A1F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A1F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a1f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A1F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a1f OCA], [http://pdbe.org/4a1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a1f RCSB], [http://www.ebi.ac.uk/pdbsum/4a1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a1f ProSAT]</span></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=4a1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a1f OCA], [https://pdbe.org/4a1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a1f RCSB], [https://www.ebi.ac.uk/pdbsum/4a1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a1f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNAB_HELPY DNAB_HELPY]] 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 (By similarity). | + | [https://www.uniprot.org/uniprot/DNAB_HELPY DNAB_HELPY] 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 (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Helicase|Helicase]] | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43504]] | + | [[Category: Helicobacter pylori]] |
| - | [[Category: DNA helicase]] | + | [[Category: Large Structures]] |
| - | [[Category: Kapp, U]] | + | [[Category: Kapp U]] |
| - | [[Category: Stelter, M]] | + | [[Category: Stelter M]] |
| - | [[Category: Terradot, L]] | + | [[Category: Terradot L]] |
| - | [[Category: Timmins, J]] | + | [[Category: Timmins J]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Dna replication]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
DNAB_HELPY 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 (By similarity).
Publication Abstract from PubMed
Hexameric DnaB helicases are often loaded at DNA replication forks by interacting with the initiator protein DnaA and/or a helicase loader (DnaC in Escherichia coli). These loaders are not universally required, and DnaB from Helicobacter pylori was found to bypass DnaC when expressed in E. coli cells. The crystal structure of Helicobacter pylori DnaB C-terminal domain (HpDnaB-CTD) reveals a large two-helix insertion (named HPI) in the ATPase domain that protrudes away from the RecA fold. Biophysical characterization and electron microscopy (EM) analysis of the full-length protein show that HpDnaB forms head-to-head double hexamers remarkably similar to helicases found in some eukaryotes, archaea, and viruses. The docking of the HpDnaB-CTD structure into EM reconstruction of HpDnaB provides a model that shows how hexamerization of the CTD is facilitated by HPI-HPI interactions. The HpDnaB double-hexamer architecture supports an alternative strategy to load bacterial helicases onto forks in the absence of helicase loaders.
Architecture of a dodecameric bacterial replicative helicase.,Stelter M, Gutsche I, Kapp U, Bazin A, Bajic G, Goret G, Jamin M, Timmins J, Terradot L Structure. 2012 Mar 7;20(3):554-64. PMID:22405014[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stelter M, Gutsche I, Kapp U, Bazin A, Bajic G, Goret G, Jamin M, Timmins J, Terradot L. Architecture of a dodecameric bacterial replicative helicase. Structure. 2012 Mar 7;20(3):554-64. PMID:22405014 doi:10.1016/j.str.2012.01.020
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