3w0f
From Proteopedia
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| - | [[ | + | ==Crystal structure of mouse Endonuclease VIII-LIKE 3 (mNEIL3)== |
| + | <StructureSection load='3w0f' size='340' side='right' caption='[[3w0f]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3w0f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W0F FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mouse, Neil3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3w0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w0f RCSB], [http://www.ebi.ac.uk/pdbsum/3w0f PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Endonuclease VIII-like 3 (Neil3) is a DNA glycosylase of the base excision repair pathway that protects cells from oxidative DNA damage by excising a broad spectrum of cytotoxic and mutagenic base lesions. Interestingly, Neil3 exhibits an unusual preference for DNA with single-stranded regions. Here, we report the 2.0 A crystal structure of a Neil3 enzyme. Although the glycosylase region of mouse Neil3 (MmuNeil3Delta324) exhibits the same overall fold as that of other Fpg/Nei proteins, it presents distinct structural features. First, MmuNeil3Delta324 lacks the alphaF-beta9/10 loop that caps the flipped-out 8-oxoG in bacterial Fpg, which is consistent with its inability to cleave 8-oxoguanine. Second, Neil3 not only lacks two of the three void-filling residues that stabilize the opposite strand, but it also harbors negatively charged residues that create an unfavorable electrostatic environment for the phosphate backbone of that strand. These structural features provide insight into the substrate specificity and marked preference of Neil3 for ssDNA. | ||
| - | + | Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNA.,Liu M, Imamura K, Averill AM, Wallace SS, Doublie S Structure. 2013 Feb 5;21(2):247-56. doi: 10.1016/j.str.2012.12.008. Epub 2013 Jan, 9. PMID:23313161<ref>PMID:23313161</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Averill, A M | + | [[Category: Averill, A M]] |
| - | [[Category: Doublie, S | + | [[Category: Doublie, S]] |
| - | [[Category: Imamura, K | + | [[Category: Imamura, K]] |
| - | [[Category: Liu, M | + | [[Category: Liu, M]] |
| - | [[Category: Wallace, S S | + | [[Category: Wallace, S S]] |
[[Category: Dna binding]] | [[Category: Dna binding]] | ||
[[Category: Helix two turns helix]] | [[Category: Helix two turns helix]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Zinc finger]] | [[Category: Zinc finger]] | ||
Revision as of 15:54, 9 December 2014
Crystal structure of mouse Endonuclease VIII-LIKE 3 (mNEIL3)
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