4xpu
From Proteopedia
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| - | ''' | + | ==The crystal structure of EndoV from E.coli== |
| + | <StructureSection load='4xpu' size='340' side='right' caption='[[4xpu]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xpu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XPU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XPU FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_V Deoxyribonuclease V], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.7 3.1.21.7] </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=4xpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xpu RCSB], [http://www.ebi.ac.uk/pdbsum/4xpu PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NFI_ECO45 NFI_ECO45]] DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Endonuclease V (EndoV) is a ubiquitous protein present in all three kingdoms of life, responsible for the specific cleavages at the second phosphodiester bond 3' to inosine. E. coli EndoV (EcEndoV) is the first member discovered in the EndoV family. It is a small protein with a compact gene organization, yet with a wide spectrum of substrate specificities. However, the structural basis of its substrate recognition is not well understood. In this study, we determined the 2.4 A crystal structure of EcEndoV. The enzyme preserves the general 'RNase H-like motif' structure. Two subunits are almost fully resolved in the asymmetric unit, but they are not related by any 2-fold axes. Rather, they establish "head-to-shoulder" contacts with loose interactions between each other. Mutational studies show that mutations that disrupt the association mode of the two subunits also decrease the cleavage efficiencies of the enzyme. Further biochemical studies suggest that EcEndoV is able to bind to single-stranded, undamaged DNA substrates without sequence specificity, and forms two types of complexes in a metal-independent manner, which may explain the wide spectrum of substrate specificities of EcEndoV. | ||
| - | + | Crystal structure of E. coli endonuclease V, an essential enzyme for deamination repair.,Zhang Z, Jia Q, Zhou C, Xie W Sci Rep. 2015 Aug 5;5:12754. doi: 10.1038/srep12754. PMID:26244280<ref>PMID:26244280</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Deoxyribonuclease V]] | ||
| + | [[Category: Xie, W]] | ||
[[Category: Zhang, Z]] | [[Category: Zhang, Z]] | ||
| - | [[Category: | + | [[Category: Dna repair]] |
| + | [[Category: Endonuclease v]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Inosine]] | ||
| + | [[Category: Rna cleavage]] | ||
Revision as of 12:12, 20 August 2015
The crystal structure of EndoV from E.coli
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