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4gop
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==Structure and Conformational Change of a Replication Protein A Heterotrimer Bound to ssDNA== |
| + | <StructureSection load='4gop' size='340' side='right' caption='[[4gop]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4gop]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ustilago_maydis_521 Ustilago maydis 521]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GOP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UM04165.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237631 Ustilago maydis 521]), UM02579.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237631 Ustilago maydis 521]), UM05156.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237631 Ustilago maydis 521])</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=4gop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gop OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gop RCSB], [http://www.ebi.ac.uk/pdbsum/4gop PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Replication protein A (RPA) is the main eukaryotic ssDNA-binding protein with essential roles in DNA replication, recombination, and repair. RPA maintains the DNA as single-stranded and also interacts with other DNA-processing proteins, coordinating their assembly and disassembly on DNA. RPA binds to ssDNA in two conformational states with opposing affinities for DNA and proteins. The RPA-protein interactions are compatible with a low DNA affinity state that involves DNA-binding domain A (DBD-A) and DBD-B but not with the high DNA affinity state that additionally engages DBD-C and DBD-D. The structure of the high-affinity RPA-ssDNA complex reported here shows a compact quaternary structure held together by a four-way interface between DBD-B, DBD-C, the intervening linker (BC linker), and ssDNA. The BC linker binds into the DNA-binding groove of DBD-B, mimicking DNA. The associated conformational change and partial occlusion of the DBD-A-DBA-B protein-protein interaction site establish a mechanism for the allosteric coupling of RPA-DNA and RPA-protein interactions. | ||
| - | + | Structure and conformational change of a replication protein A heterotrimer bound to ssDNA.,Fan J, Pavletich NP Genes Dev. 2012 Oct 15;26(20):2337-47. doi: 10.1101/gad.194787.112. PMID:23070815<ref>PMID:23070815</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Ustilago maydis 521]] | [[Category: Ustilago maydis 521]] | ||
| - | [[Category: Jie, F | + | [[Category: Jie, F]] |
| - | [[Category: Pavletich, N P | + | [[Category: Pavletich, N P]] |
[[Category: Dna binding protein-dna complex]] | [[Category: Dna binding protein-dna complex]] | ||
[[Category: Ob fold]] | [[Category: Ob fold]] | ||
[[Category: Ssdna binding]] | [[Category: Ssdna binding]] | ||
Revision as of 09:37, 10 December 2014
Structure and Conformational Change of a Replication Protein A Heterotrimer Bound to ssDNA
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