1zp7
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1zp7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZP7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1zp7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZP7 FirstGlance]. <br> | ||
| - | </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=1zp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zp7 OCA], [https://pdbe.org/1zp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zp7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zp7 ProSAT]</span></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]] 2.25Å</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=1zp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zp7 OCA], [https://pdbe.org/1zp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zp7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zp7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RECU_BACSU RECU_BACSU] Has at least 2 separable functions; Holliday junction resolution with generation of monomeric chromosomes, and modulation of RecA activity. Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. Partially inhibits the hydrolysis of dATP or rATP by RecA. Holliday junction resolution is stimulated by RuvB.<ref>PMID:14701911</ref> <ref>PMID:16020779</ref> <ref>PMID:16154091</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zp7 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zp7 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We have determined the structure of the enzyme RecU from Bacillus subtilis, that is the general Holliday junction resolving enzyme in Gram-positive bacteria. The enzyme fold reveals a striking similarity to a class of resolvase enzymes found in archaeal sources and members of the type II restriction endonuclease family to which they are related. The structure confirms the presence of active sites formed around clusters of acidic residues that we have also shown to bind divalent cations. Mutagenesis data presented here support the key role of certain residues. The RecU structure suggests a basis for Holliday junction selectivity and suggests how sequence-specific cleavage might be achieved. Models for a resolvase-DNA complex address how the enzyme might organize junctions into an approximately 4-fold symmetric form. | ||
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| - | The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence-specific cleavage.,McGregor N, Ayora S, Sedelnikova S, Carrasco B, Alonso JC, Thaw P, Rafferty J Structure. 2005 Sep;13(9):1341-51. PMID:16154091<ref>PMID:16154091</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1zp7" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Alonso | + | [[Category: Alonso JC]] |
| - | [[Category: Ayora | + | [[Category: Ayora S]] |
| - | [[Category: Carrasco | + | [[Category: Carrasco B]] |
| - | [[Category: McGregor | + | [[Category: McGregor N]] |
| - | [[Category: Rafferty | + | [[Category: Rafferty J]] |
| - | [[Category: Sedelnikova | + | [[Category: Sedelnikova S]] |
| - | [[Category: Thaw | + | [[Category: Thaw P]] |
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Current revision
The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence specific cleavage.
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