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| | ==Structure of T4 Bacteriophage Clamp Loader Bound To Open Clamp, DNA and ATP Analog== | | ==Structure of T4 Bacteriophage Clamp Loader Bound To Open Clamp, DNA and ATP Analog== |
| - | <StructureSection load='3u60' size='340' side='right' caption='[[3u60]], [[Resolution|resolution]] 3.34Å' scene=''> | + | <StructureSection load='3u60' size='340' side='right'caption='[[3u60]], [[Resolution|resolution]] 3.34Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3u60]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U60 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3u60]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U60 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.34Å</td></tr> |
| - | <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>
| + | <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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1czd|1czd]], [[1sxj|1sxj]], [[3glf|3glf]], [[1jr3|1jr3]], [[1xxh|1xxh]], [[3u5z|3u5z]], [[3u61|3u61]]</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=3u60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u60 OCA], [https://pdbe.org/3u60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u60 RCSB], [https://www.ebi.ac.uk/pdbsum/3u60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u60 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">44, gp44 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), 62, gp62 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), 45, gp45 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u60 OCA], [http://pdbe.org/3u60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u60 RCSB], [http://www.ebi.ac.uk/pdbsum/3u60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u60 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[http://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> [[http://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/LOADL_BPT4 LOADL_BPT4] Forms the sliding-clamp-loader together with the small subunit (PubMed:10585481). Functions as an ATPase enzyme (PubMed:16800623, PubMed:18676368). The clamp loader holds the clamp in an open conformation and places it onto the DNA (PubMed:18676368, PubMed:22194570). 4 ATP molecules must bind to the sliding-clamp-loader before the latter can open the sliding clamp (PubMed:18676368). ATP hydrolysis triggers the detachment of the sliding clamp from the sliding-clamp-loader, freeing the sliding clamp to track along DNA (PubMed:18676368, PubMed:22194570).[HAMAP-Rule:MF_04162]<ref>PMID:10585481</ref> <ref>PMID:16800623</ref> <ref>PMID:18676368</ref> <ref>PMID:22194570</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpt4]] | + | [[Category: Escherichia virus T4]] |
| - | [[Category: Donnell, M O]] | + | [[Category: Large Structures]] |
| - | [[Category: Kelch, B A]] | + | [[Category: Kelch BA]] |
| - | [[Category: Kuriyan, J]] | + | [[Category: Kuriyan J]] |
| - | [[Category: Makino, D L]] | + | [[Category: Makino DL]] |
| - | [[Category: Aaa+]] | + | [[Category: O'Donnell M]] |
| - | [[Category: Atp hydrolase]]
| + | |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Sliding clamp]]
| + | |
| Structural highlights
Function
LOADL_BPT4 Forms the sliding-clamp-loader together with the small subunit (PubMed:10585481). Functions as an ATPase enzyme (PubMed:16800623, PubMed:18676368). The clamp loader holds the clamp in an open conformation and places it onto the DNA (PubMed:18676368, PubMed:22194570). 4 ATP molecules must bind to the sliding-clamp-loader before the latter can open the sliding clamp (PubMed:18676368). ATP hydrolysis triggers the detachment of the sliding clamp from the sliding-clamp-loader, freeing the sliding clamp to track along DNA (PubMed:18676368, PubMed:22194570).[HAMAP-Rule:MF_04162][1] [2] [3] [4]
Publication Abstract from PubMed
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.
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Janzen DM, Torgov MY, Reddy MK. In vitro reconstitution of the bacteriophage T4 clamp loader complex (gp44/62). J Biol Chem. 1999 Dec 10;274(50):35938-43. PMID:10585481 doi:10.1074/jbc.274.50.35938
- ↑ Zhuang Z, Berdis AJ, Benkovic SJ. An alternative clamp loading pathway via the T4 clamp loader gp44/62-DNA complex. Biochemistry. 2006 Jul 4;45(26):7976-89. PMID:16800623 doi:http://dx.doi.org/10.1021/bi0601205
- ↑ Pietroni P, von Hippel PH. Multiple ATP binding is required to stabilize the "activated" (clamp open) clamp loader of the T4 DNA replication complex. J Biol Chem. 2008 Oct 17;283(42):28338-53. doi: 10.1074/jbc.M804371200. Epub 2008, Aug 1. PMID:18676368 doi:http://dx.doi.org/10.1074/jbc.M804371200
- ↑ Kelch BA, Makino DL, O'Donnell M, Kuriyan J. How a DNA polymerase clamp loader opens a sliding clamp. Science. 2011 Dec 23;334(6063):1675-80. PMID:22194570 doi:10.1126/science.1211884
- ↑ Kelch BA, Makino DL, O'Donnell M, Kuriyan J. How a DNA polymerase clamp loader opens a sliding clamp. Science. 2011 Dec 23;334(6063):1675-80. PMID:22194570 doi:10.1126/science.1211884
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