1clq

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(New page: 200px<br /> <applet load="1clq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1clq, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1clq.gif|left|200px]]<br />
 
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<applet load="1clq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1clq, resolution 2.70&Aring;" />
 
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'''CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION==
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We have solved the crystal structures of the bacteriophage RB69 sliding, clamp, its complex with a peptide essential for DNA polymerase, interactions, and the DNA polymerase complexed with primer-template DNA., The editing complex structure shows a partially melted duplex DNA exiting, from the exonuclease domain at an unexpected angle and significant changes, in the protein structure. The clamp complex shows the C-terminal 11, residues of polymerase bound in a hydrophobic pocket, and it allows, docking of the editing and clamp structures together. The peptide binds to, the sliding clamp at a position identical to that of a replication, inhibitor peptide bound to PCNA, suggesting that the replication inhibitor, protein p21CIP1 functions by competing with eukaryotic polymerases for the, same binding pocket on the clamp.
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<StructureSection load='1clq' size='340' side='right'caption='[[1clq]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1clq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. The March 2000 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''DNA Polymerase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2000_3 10.2210/rcsb_pdb/mom_2000_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CLQ FirstGlance]. <br>
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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]] 2.7&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></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=1clq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clq OCA], [https://pdbe.org/1clq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1clq RCSB], [https://www.ebi.ac.uk/pdbsum/1clq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1clq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DPOL_BPR69 DPOL_BPR69] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.
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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/cl/1clq_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=1clq 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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We have solved the crystal structures of the bacteriophage RB69 sliding clamp, its complex with a peptide essential for DNA polymerase interactions, and the DNA polymerase complexed with primer-template DNA. The editing complex structure shows a partially melted duplex DNA exiting from the exonuclease domain at an unexpected angle and significant changes in the protein structure. The clamp complex shows the C-terminal 11 residues of polymerase bound in a hydrophobic pocket, and it allows docking of the editing and clamp structures together. The peptide binds to the sliding clamp at a position identical to that of a replication inhibitor peptide bound to PCNA, suggesting that the replication inhibitor protein p21CIP1 functions by competing with eukaryotic polymerases for the same binding pocket on the clamp.
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==About this Structure==
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Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex.,Shamoo Y, Steitz TA Cell. 1999 Oct 15;99(2):155-66. PMID:10535734<ref>PMID:10535734</ref>
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1CLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_rb18 Enterobacteria phage rb18] with CA and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1CLQ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb3_1.html DNA Polymerase]]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CLQ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex., Shamoo Y, Steitz TA, Cell. 1999 Oct 15;99(2):155-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10535734 10535734]
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</div>
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[[Category: DNA Polymerase]]
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<div class="pdbe-citations 1clq" style="background-color:#fffaf0;"></div>
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[[Category: DNA-directed DNA polymerase]]
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[[Category: Enterobacteria phage rb18]]
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[[Category: Single protein]]
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[[Category: Shamoo, Y.]]
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[[Category: Steitz, T.A.]]
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[[Category: CA]]
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[[Category: GDP]]
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[[Category: dna polymerase]]
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[[Category: editing]]
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[[Category: gp43]]
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[[Category: proofreading]]
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[[Category: replication]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 08:58:26 2007''
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==See Also==
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: DNA Polymerase]]
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[[Category: Escherichia phage RB69]]
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[[Category: Large Structures]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Shamoo Y]]
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[[Category: Steitz TA]]

Current revision

CRYSTAL STRUCTURE OF A REPLICATION FORK DNA POLYMERASE EDITING COMPLEX AT 2.7 A RESOLUTION

PDB ID 1clq

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