1oyy

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[[Image:1oyy.jpg|left|200px]]
 
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==Structure of the RecQ Catalytic Core bound to ATP-gamma-S==
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The line below this paragraph, containing "STRUCTURE_1oyy", creates the "Structure Box" on the page.
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<StructureSection load='1oyy' size='340' side='right'caption='[[1oyy]], [[Resolution|resolution]] 2.50&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'>[[1oyy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OYY 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]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1oyy| PDB=1oyy | SCENE= }}
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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=1oyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyy OCA], [https://pdbe.org/1oyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oyy RCSB], [https://www.ebi.ac.uk/pdbsum/1oyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oyy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RECQ_ECOLI RECQ_ECOLI] Involved in the RecF recombination pathway; its gene expression is under the regulation of the SOS system. It is a DNA helicase.
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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/oy/1oyy_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=1oyy 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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RecQ family helicases catalyze critical genome maintenance reactions in bacterial and eukaryotic cells, playing key roles in several DNA metabolic processes. Mutations in recQ genes are linked to genome instability and human disease. To define the physical basis of RecQ enzyme function, we have determined a 1.8 A resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of the core bound to the ATP analog ATPgammaS. The RecQ core comprises four conserved subdomains; two of these combine to form its helicase region, while the others form unexpected Zn(2+)-binding and winged-helix motifs. The structures reveal the molecular basis of missense mutations that cause Bloom's syndrome, a human RecQ-associated disease. Finally, based on findings from the structures, we propose a mechanism for RecQ activity that could explain its functional coordination with topoisomerase III.
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'''Structure of the RecQ Catalytic Core bound to ATP-gamma-S'''
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High-resolution structure of the E.coli RecQ helicase catalytic core.,Bernstein DA, Zittel MC, Keck JL EMBO J. 2003 Oct 1;22(19):4910-21. PMID:14517231<ref>PMID:14517231</ref>
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==Overview==
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RecQ family helicases catalyze critical genome maintenance reactions in bacterial and eukaryotic cells, playing key roles in several DNA metabolic processes. Mutations in recQ genes are linked to genome instability and human disease. To define the physical basis of RecQ enzyme function, we have determined a 1.8 A resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of the core bound to the ATP analog ATPgammaS. The RecQ core comprises four conserved subdomains; two of these combine to form its helicase region, while the others form unexpected Zn(2+)-binding and winged-helix motifs. The structures reveal the molecular basis of missense mutations that cause Bloom's syndrome, a human RecQ-associated disease. Finally, based on findings from the structures, we propose a mechanism for RecQ activity that could explain its functional coordination with topoisomerase III.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1OYY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYY OCA].
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</div>
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<div class="pdbe-citations 1oyy" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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High-resolution structure of the E.coli RecQ helicase catalytic core., Bernstein DA, Zittel MC, Keck JL, EMBO J. 2003 Oct 1;22(19):4910-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14517231 14517231]
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*[[Helicase 3D structures|Helicase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bernstein, D A.]]
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[[Category: Bernstein DA]]
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[[Category: Keck, J L.]]
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[[Category: Keck JL]]
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[[Category: Zittel, M C.]]
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[[Category: Zittel MC]]
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[[Category: Atp binding]]
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[[Category: Helicase]]
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[[Category: Helix-turn-helix]]
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[[Category: Recq]]
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[[Category: Winged helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:27:00 2008''
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Current revision

Structure of the RecQ Catalytic Core bound to ATP-gamma-S

PDB ID 1oyy

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