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3sav
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sav]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SAV FirstGlance]. <br> | <table><tr><td colspan='2'>[[3sav]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SAV FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CX2:2-DEOXY-5-O-{(R)-HYDROXY[(2-SULFANYLETHYL)AMINO]PHOSPHORYL}CYTIDINE'>CX2</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CX2:2-DEOXY-5-O-{(R)-HYDROXY[(2-SULFANYLETHYL)AMINO]PHOSPHORYL}CYTIDINE'>CX2</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sar|3sar]], [[3sas|3sas]], [[3sat|3sat]], [[3sau|3sau]], [[3saw|3saw]], [[3sbj|3sbj]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sar|3sar]], [[3sas|3sas]], [[3sat|3sat]], [[3sau|3sau]], [[3saw|3saw]], [[3sbj|3sbj]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUTM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUTM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-(apurinic_or_apyrimidinic_site)_lyase DNA-(apurinic or apyrimidinic site) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-(apurinic_or_apyrimidinic_site)_lyase DNA-(apurinic or apyrimidinic site) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sav OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sav RCSB], [http://www.ebi.ac.uk/pdbsum/3sav PDBsum]</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=3sav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sav OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sav RCSB], [http://www.ebi.ac.uk/pdbsum/3sav PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/P84131_GEOSE P84131_GEOSE]] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity).[HAMAP-Rule:MF_00103][SAAS:SAAS020629_004_120556] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Strandwise translocation of a DNA glycosylase on undamaged DNA.,Qi Y, Nam K, Spong MC, Banerjee A, Sung RJ, Zhang M, Karplus M, Verdine GL Proc Natl Acad Sci U S A. 2012 Jan 24;109(4):1086-91. Epub 2012 Jan 4. PMID:22219368<ref>PMID:22219368</ref> | Strandwise translocation of a DNA glycosylase on undamaged DNA.,Qi Y, Nam K, Spong MC, Banerjee A, Sung RJ, Zhang M, Karplus M, Verdine GL Proc Natl Acad Sci U S A. 2012 Jan 24;109(4):1086-91. Epub 2012 Jan 4. PMID:22219368<ref>PMID:22219368</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[DNA glycosylase|DNA glycosylase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
| - | [[Category: Qi, Y | + | [[Category: Qi, Y]] |
| - | [[Category: Spong, M C | + | [[Category: Spong, M C]] |
| - | [[Category: Verdine, G L | + | [[Category: Verdine, G L]] |
[[Category: Damage search]] | [[Category: Damage search]] | ||
[[Category: Disulfide crosslinking]] | [[Category: Disulfide crosslinking]] | ||
Revision as of 01:43, 25 December 2014
MUTM Slanted complex 8
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Categories: Geobacillus stearothermophilus | Qi, Y | Spong, M C | Verdine, G L | Damage search | Disulfide crosslinking | Dna damage | Dna glycosylase | Dna repair | Dna-binding | Glycosidase | Hydrolase | Hydrolase-dna complex | Lyase | Metal-binding | Multifunctional enzyme | Translocation | Zinc-finger
