|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4xpu' size='340' side='right'caption='[[4xpu]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='4xpu' size='340' side='right'caption='[[4xpu]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xpu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco45 Eco45]. 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> | + | <table><tr><td colspan='2'>[[4xpu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_S88 Escherichia coli S88]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4XPU FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nfi, ECS88_4459 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585035 ECO45])</td></tr> | + | </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=4xpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpu OCA], [https://pdbe.org/4xpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xpu RCSB], [https://www.ebi.ac.uk/pdbsum/4xpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xpu ProSAT]</span></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://pdbe.org/4xpu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xpu RCSB], [http://www.ebi.ac.uk/pdbsum/4xpu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xpu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 19: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Endonuclease|Endonuclease]] | + | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Deoxyribonuclease V]] | + | [[Category: Escherichia coli S88]] |
| - | [[Category: Eco45]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xie, W]] | + | [[Category: Xie W]] |
| - | [[Category: Zhang, Z]] | + | [[Category: Zhang Z]] |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Endonuclease v]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inosine]]
| + | |
| - | [[Category: Rna cleavage]]
| + | |
| Structural highlights
Function
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang Z, Jia Q, Zhou C, Xie W. Crystal structure of E. coli endonuclease V, an essential enzyme for deamination repair. Sci Rep. 2015 Aug 5;5:12754. doi: 10.1038/srep12754. PMID:26244280 doi:http://dx.doi.org/10.1038/srep12754
|
