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4lyl
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lyl]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LYL FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lyl]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LYL FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1okb|1okb]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1okb|1okb]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] </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=4lyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lyl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lyl RCSB], [http://www.ebi.ac.uk/pdbsum/4lyl 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=4lyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lyl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lyl RCSB], [http://www.ebi.ac.uk/pdbsum/4lyl PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q9I983_GADMO Q9I983_GADMO]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine (By similarity).[RuleBase:RU003780][HAMAP-Rule:MF_03166] [[http://www.uniprot.org/uniprot/UNGI_BPPB2 UNGI_BPPB2]] This protein binds specifically and reversibly to the host uracil-DNA glycosylase, preventing removal of uracil residues from PBS2 DNA by the host uracil-excision repair system. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Uridine nucleosidase]] | [[Category: Uridine nucleosidase]] | ||
| - | [[Category: Assefa, N G | + | [[Category: Assefa, N G]] |
| - | [[Category: Johnson, K A | + | [[Category: Johnson, K A]] |
| - | [[Category: Leiros, H K.S | + | [[Category: Leiros, H K.S]] |
| - | [[Category: Moe, E | + | [[Category: Moe, E]] |
| - | [[Category: Niiranen, L M.K | + | [[Category: Niiranen, L M.K]] |
| - | [[Category: Smalas, A O | + | [[Category: Smalas, A O]] |
| - | [[Category: Willassen, N P | + | [[Category: Willassen, N P]] |
[[Category: Alpha/beta fold]] | [[Category: Alpha/beta fold]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: Hydrolysis]] | [[Category: Hydrolysis]] | ||
[[Category: Intracellular]] | [[Category: Intracellular]] | ||
Revision as of 15:17, 25 December 2014
Crystal structure of uracil-DNA glycosylase from cod (Gadus morhua) in complex with the proteinaceous inhibitor UGI
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