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3qea
From Proteopedia
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| - | [[ | + | ==Crystal structure of human exonuclease 1 Exo1 (WT) in complex with DNA (complex II)== |
| + | <StructureSection load='3qea' size='340' side='right' caption='[[3qea]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3qea]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QEA FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qe9|3qe9]], [[3qeb|3qeb]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXO1, EXOI, HEX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3qea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qea OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qea RCSB], [http://www.ebi.ac.uk/pdbsum/3qea PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human exonuclease 1 (hExo1) plays important roles in DNA repair and recombination processes that maintain genomic integrity. It is a member of the 5' structure-specific nuclease family of exonucleases and endonucleases that includes FEN-1, XPG, and GEN1. We present structures of hExo1 in complex with a DNA substrate, followed by mutagenesis studies, and propose a common mechanism by which this nuclease family recognizes and processes diverse DNA structures. hExo1 induces a sharp bend in the DNA at nicks or gaps. Frayed 5' ends of nicked duplexes resemble flap junctions, unifying the mechanisms of endo- and exonucleolytic processing. Conformational control of a mobile region in the catalytic site suggests a mechanism for allosteric regulation by binding to protein partners. The relative arrangement of substrate binding sites in these enzymes provides an elegant solution to a complex geometrical puzzle of substrate recognition and processing. | ||
| - | + | Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family.,Orans J, McSweeney EA, Iyer RR, Hast MA, Hellinga HW, Modrich P, Beese LS Cell. 2011 Apr 15;145(2):212-23. PMID:21496642<ref>PMID:21496642</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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| - | + | ||
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==See Also== | ==See Also== | ||
*[[Exonuclease|Exonuclease]] | *[[Exonuclease|Exonuclease]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Beese, L S | + | [[Category: Beese, L S]] |
| - | [[Category: Hast, M A | + | [[Category: Hast, M A]] |
| - | [[Category: Hellinga, H W | + | [[Category: Hellinga, H W]] |
| - | [[Category: Iyer, R R | + | [[Category: Iyer, R R]] |
| - | [[Category: McSweeney, E A | + | [[Category: McSweeney, E A]] |
| - | [[Category: Modrich, P | + | [[Category: Modrich, P]] |
| - | [[Category: Orans, J | + | [[Category: Orans, J]] |
[[Category: Exonuclease]] | [[Category: Exonuclease]] | ||
[[Category: Hydrolase-dna complex]] | [[Category: Hydrolase-dna complex]] | ||
Revision as of 12:04, 9 December 2014
Crystal structure of human exonuclease 1 Exo1 (WT) in complex with DNA (complex II)
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