2a1k: Difference between revisions
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<StructureSection load='2a1k' size='340' side='right'caption='[[2a1k]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2a1k' size='340' side='right'caption='[[2a1k]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a1k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2a1k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A1K FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2a1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a1k OCA], [https://pdbe.org/2a1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a1k RCSB], [https://www.ebi.ac.uk/pdbsum/2a1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a1k ProSAT]</span></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=2a1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a1k OCA], [https://pdbe.org/2a1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a1k RCSB], [https://www.ebi.ac.uk/pdbsum/2a1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a1k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7Y265_BPR69 Q7Y265_BPR69] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia phage RB69]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Geng | [[Category: Geng L]] | ||
[[Category: Shamoo | [[Category: Shamoo Y]] | ||
[[Category: Sun | [[Category: Sun S]] | ||
Latest revision as of 10:17, 23 August 2023
RB69 single-stranded DNA binding protein core domainRB69 single-stranded DNA binding protein core domain
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn vivo, replicative DNA polymerases are made more processive by their interactions with accessory proteins at the replication fork. Single-stranded DNA binding protein (SSB) is an essential protein that binds tightly and cooperatively to single-stranded DNA during replication to remove adventitious secondary structures and protect the exposed DNA from endogenous nucleases. Using information from high resolution structures and biochemical data, we have engineered a functional chimeric enzyme of the bacteriophage RB69 DNA polymerase and SSB with substantially increased processivity. Fusion of RB69 DNA polymerase with its cognate SSB via a short six amino acid linker increases affinity for primer-template DNA by sixfold and subsequently increases processivity by sevenfold while maintaining fidelity. The crystal structure of this fusion protein was solved by a combination of multiwavelength anomalous diffraction and molecular replacement to 3.2 A resolution and shows that RB69 SSB is positioned proximal to the N-terminal domain of RB69 DNA polymerase near the template strand channel. The structural and biochemical data suggest that SSB interactions with DNA polymerase are transient and flexible, consistent with models of a dynamic replisome during elongation. Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity.,Sun S, Geng L, Shamoo Y Proteins. 2006 Oct 1;65(1):231-8. PMID:16881051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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