1qhh: Difference between revisions

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-[[Image:1qhh.jpg|left|200px]]
- {{Structure
+==STRUCTURE OF DNA HELICASE WITH ADPNP==
-|PDB= 1qhh |SIZE=350|CAPTION= <scene name='initialview01'>1qhh</scene>, resolution 2.5&Aring;
+<StructureSection load='1qhh' size='340' side='right'caption='[[1qhh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
+<table><tr><td colspan='2'>[[1qhh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QHH FirstGlance]. <br>
-|ACTIVITY=
+</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>
-|GENE= PCRA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></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=1qhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qhh OCA], [https://pdbe.org/1qhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qhh RCSB], [https://www.ebi.ac.uk/pdbsum/1qhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qhh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PCRA_GEOSE PCRA_GEOSE] DNA helicase. Has a broad nucleotide specificity, even being able to hydrolyze ethenonucleotides, and is able to couple the hydrolysis to unwinding of DNA substrates. It is a 3'-5' helicase but at high protein concentrations it can also displace a substrate with a 5' tail. Preferred substrate being one with both single and double-stranded regions of DNA.
+== 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/qh/1qhh_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=1qhh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Based upon the crystal structures of PcrA helicase, we have made and characterised mutations in a number of conserved helicase signature motifs around the ATPase active site. We have also determined structures of complexes of wild-type PcrA with ADPNP and of a mutant PcrA complexed with ADPNP and Mn2+. The kinetic and structural data define roles for a number of different residues in and around the ATP binding site. More importantly, our results also show that there are two functionally distinct conformations of ATP in the active site. In one conformation, ATP is hydrolysed poorly whereas in the other (activated) conformation, ATP is hydrolysed much more rapidly. We propose a mechanism to explain how the stimulation of ATPase activity afforded by binding of single-stranded DNA stabilises the activated conformation favouring Mg2+binding and a consequent repositioning of the gamma-phosphate group which promotes ATP hydrolysis. A part of the associated conformational change in the protein forces the side-chain of K37 to vacate the Mg2+binding site, allowing the cation to bind and interact with ATP.
-'''STRUCTURE OF DNA HELICASE WITH ADPNP'''
+DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase.,Soultanas P, Dillingham MS, Velankar SS, Wigley DB J Mol Biol. 1999 Jul 2;290(1):137-48. PMID:10388562<ref>PMID:10388562</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1qhh" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Based upon the crystal structures of PcrA helicase, we have made and characterised mutations in a number of conserved helicase signature motifs around the ATPase active site. We have also determined structures of complexes of wild-type PcrA with ADPNP and of a mutant PcrA complexed with ADPNP and Mn2+. The kinetic and structural data define roles for a number of different residues in and around the ATP binding site. More importantly, our results also show that there are two functionally distinct conformations of ATP in the active site. In one conformation, ATP is hydrolysed poorly whereas in the other (activated) conformation, ATP is hydrolysed much more rapidly. We propose a mechanism to explain how the stimulation of ATPase activity afforded by binding of single-stranded DNA stabilises the activated conformation favouring Mg2+binding and a consequent repositioning of the gamma-phosphate group which promotes ATP hydrolysis. A part of the associated conformational change in the protein forces the side-chain of K37 to vacate the Mg2+binding site, allowing the cation to bind and interact with ATP.
+*[[Helicase 3D structures|Helicase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-QHH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHH OCA].
+__TOC__
+</StructureSection>
-==Reference==
-DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase., Soultanas P, Dillingham MS, Velankar SS, Wigley DB, J Mol Biol. 1999 Jul 2;290(1):137-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10388562 10388562]
 [[Category: Geobacillus stearothermophilus]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Dillingham, M S.]]
+[[Category: Dillingham MS]]
-[[Category: Soultanas, P.]]
+[[Category: Soultanas P]]
-[[Category: Velankar, S S.]]
+[[Category: Velankar SS]]
-[[Category: Wigley, D B.]]
+[[Category: Wigley DB]]
-[[Category: ATP]]
-[[Category: atp-binding]]
-[[Category: dna repair]]
-[[Category: dna replication]]
-[[Category: dna-binding]]
-[[Category: helicase]]
-[[Category: sos response]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:37:31 2008''