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3u5z

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'''Unreleased structure'''
 
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The entry 3u5z is ON HOLD
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==Structure of T4 Bacteriophage clamp loader bound to the T4 clamp, primer-template DNA, and ATP analog==
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<StructureSection load='3u5z' size='340' side='right'caption='[[3u5z]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3u5z]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. The June 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Sliding Clamps'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_6 10.2210/rcsb_pdb/mom_2012_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U5Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=08T:[[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-TRIS(FLUORANYL)BERYLLIUM'>08T</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1czd|1czd]], [[1sxj|1sxj]], [[3glf|3glf]], [[1jr3|1jr3]], [[1xxh|1xxh]], [[3u60|3u60]], [[3u61|3u61]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">44, gp44 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), 62, gp62 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), 45, gp45 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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=3u5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u5z OCA], [https://pdbe.org/3u5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u5z RCSB], [https://www.ebi.ac.uk/pdbsum/3u5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u5z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/DPA44_BPT4 DPA44_BPT4]] Function as a sliding-clamp-loading ATPase enzyme during DNA replication. Required for elongation of primed templates by controlling the polymerase processivity. Possesses DNA-dependent ATPase activity on its own and within the heterodimer gp44/gp62. Progressive binding of ATPs triggers a conformational change in the complex that inhibits ATPase activity.<ref>PMID:16800623</ref> <ref>PMID:18676368</ref> [[https://www.uniprot.org/uniprot/DPA5_BPT4 DPA5_BPT4]] Replisome sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. [[https://www.uniprot.org/uniprot/DPA62_BPT4 DPA62_BPT4]] Function as a sliding-clamp-loading ATPase enzyme during DNA replication. Required for elongation of primed templates by controlling the polymerase processivity. Progressive binding of ATPs triggers a conformational change in the complex that inhibits ATPase activity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Processive chromosomal replication relies on sliding DNA clamps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of adenosine triphosphatases (ATPases). We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template DNA. The clamp loader traps a spiral conformation of the open clamp so that both the loader and the clamp match the helical symmetry of DNA. One structure reveals that ATP has been hydrolyzed in one subunit and suggests that clamp closure and ejection of the loader involves disruption of the ATP-dependent match in symmetry. The structures explain how synergy among the loader, the clamp, and DNA can trigger ATP hydrolysis and release of the closed clamp on DNA.
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Authors: Kelch, B.A., Makino, D.L., O'Donnell, M., Kuriyan, J.
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How a DNA polymerase clamp loader opens a sliding clamp.,Kelch BA, Makino DL, O'Donnell M, Kuriyan J Science. 2011 Dec 23;334(6063):1675-80. PMID:22194570<ref>PMID:22194570</ref>
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Description: Structure of T4 Bacteriophage clamp loader bound to the T4 clamp, primer-template DNA, and ATP analog
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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 3u5z" style="background-color:#fffaf0;"></div>
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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: Bpt4]]
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[[Category: Large Structures]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Sliding Clamps]]
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[[Category: Donnell, M O]]
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[[Category: Kelch, B A]]
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[[Category: Kuriyan, J]]
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[[Category: Makino, D L]]
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[[Category: Aaa+]]
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[[Category: Atp hydrolase]]
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[[Category: Clamp loader]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Sliding clamp]]

Current revision

Structure of T4 Bacteriophage clamp loader bound to the T4 clamp, primer-template DNA, and ATP analog

PDB ID 3u5z

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