3gxv

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{{Seed}}
 
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[[Image:3gxv.jpg|left|200px]]
 
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==Three-dimensional structure of N-terminal domain of DnaB Helicase from Helicobacter pylori and its interactions with primase==
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The line below this paragraph, containing "STRUCTURE_3gxv", creates the "Structure Box" on the page.
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<StructureSection load='3gxv' size='340' side='right'caption='[[3gxv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3gxv]] is a 4 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=3GXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GXV FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#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=3gxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxv OCA], [https://pdbe.org/3gxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gxv RCSB], [https://www.ebi.ac.uk/pdbsum/3gxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gxv ProSAT]</span></td></tr>
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{{STRUCTURE_3gxv| PDB=3gxv | SCENE= }}
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/3gxv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3gxv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Replication initiation is a crucial step in genome duplication and homohexameric DnaB helicase plays a central role in the replication initiation process by unwinding the duplex DNA and interacting with several other proteins during the process of replication. N-terminal domain of DnaB is critical for helicase activity and for DnaG primase interactions. We present here the crystal structure of the N-terminal domain (NTD) of H. pylori DnaB (HpDnaB) helicase at 2.2 A resolution and compare the structural differences among helicases and correlate with the functional differences. The structural details of NTD suggest that the linker region between NTD and C-terminal helicase domain plays a vital role in accurate assembly of NTD dimers. The sequence analysis of the linker regions from several helicases reveals that they should form four helix bundles. We also report the characterization of H. pylori DnaG primase and study the helicase-primase interactions, where HpDnaG primase stimulates DNA unwinding activity of HpDnaB suggesting presence of helicase-primase cohort at the replication fork. The protein-protein interaction study of C-terminal domain of primase and different deletion constructs of helicase suggests that linker is essential for proper conformation of NTD to interact strongly with HpDnaG. The surface charge distribution on the primase binding surface of NTDs of various helicases suggests that DnaB-DnaG interaction and stability of the complex is most probably charge dependent. Structure of the linker and helicase-primase interactions indicate that HpDnaB differs greatly from E.coli DnaB despite both belong to gram negative bacteria.
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===Three-dimensional structure of N-terminal domain of DnaB Helicase from Helicobacter pylori and its interactions with primase===
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Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori.,Kashav T, Nitharwal R, Abdulrehman SA, Gabdoulkhakov A, Saenger W, Dhar SK, Gourinath S PLoS One. 2009 Oct 20;4(10):e7515. PMID:19841750<ref>PMID:19841750</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3gxv" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19841750}}, adds the Publication Abstract to the page
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*[[Helicase 3D structures|Helicase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19841750 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19841750}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3GXV is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXV OCA].
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==Reference==
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<ref group="xtra">PMID:19841750</ref><references group="xtra"/>
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[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
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[[Category: Dhar, K S.]]
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[[Category: Large Structures]]
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[[Category: Gabdoulkhakov, A.]]
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[[Category: Dhar KS]]
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[[Category: Gourinath, S.]]
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[[Category: Gabdoulkhakov A]]
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[[Category: Kashav, T.]]
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[[Category: Gourinath S]]
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[[Category: Nitharwal, R.]]
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[[Category: Kashav T]]
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[[Category: Saenger, W.]]
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[[Category: Nitharwal R]]
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[[Category: Syed, A A.]]
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[[Category: Saenger W]]
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[[Category: Atp-binding]]
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[[Category: Syed AA]]
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[[Category: Autocatalytic cleavage]]
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[[Category: Dna replication]]
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[[Category: Dna-binding]]
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[[Category: Dna-binding hydrolase]]
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[[Category: Helicase]]
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[[Category: Helicobacter pylori]]
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[[Category: Hexameric helicase]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase/replication complex]]
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[[Category: Nucleotide-binding]]
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[[Category: Primase]]
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[[Category: Primosome]]
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[[Category: Replication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 27 19:30:45 2010''
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Current revision

Three-dimensional structure of N-terminal domain of DnaB Helicase from Helicobacter pylori and its interactions with primase

PDB ID 3gxv

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