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==Structure of T4 Bacteriophage Clamp Loader Bound To Closed Clamp, DNA and ATP Analog and ADP== | ==Structure of T4 Bacteriophage Clamp Loader Bound To Closed Clamp, DNA and ATP Analog and ADP== | ||
<StructureSection load='3u61' size='340' side='right' caption='[[3u61]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='3u61' size='340' side='right' caption='[[3u61]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3u61]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3u61]] 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=3U61 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U61 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='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> | ||
<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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1czd|1czd]], [[1jr3|1jr3]], [[1sxj|1sxj]], [[1xxh|1xxh]], [[1xxi|1xxi]], [[3glf|3glf]], [[3glg|3glg]], [[3u5z|3u5z]], [[3u60|3u60]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1czd|1czd]], [[1jr3|1jr3]], [[1sxj|1sxj]], [[1xxh|1xxh]], [[1xxi|1xxi]], [[3glf|3glf]], [[3glg|3glg]], [[3u5z|3u5z]], [[3u60|3u60]]</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 | <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=3u61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u61 RCSB], [http://www.ebi.ac.uk/pdbsum/3u61 PDBsum]</span></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=3u61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u61 OCA], [http://pdbe.org/3u61 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u61 RCSB], [http://www.ebi.ac.uk/pdbsum/3u61 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u61 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[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. | [[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. [[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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3u61" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bpt4]] | ||
[[Category: Donnell, M O]] | [[Category: Donnell, M O]] | ||
[[Category: Kelch, B A]] | [[Category: Kelch, B A]] | ||
Revision as of 05:17, 5 August 2016
Structure of T4 Bacteriophage Clamp Loader Bound To Closed Clamp, DNA and ATP Analog and ADPStructure of T4 Bacteriophage Clamp Loader Bound To Closed Clamp, DNA and ATP Analog and ADP
Structural highlights
Function[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.[1] [2] [DPA5_BPT4] Replisome sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. [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. Publication Abstract from PubMedProcessive 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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