1oe6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:46, 17 April 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Xenopus SMUG1, an anti-mutator uracil-DNA Glycosylase==
==Xenopus SMUG1, an anti-mutator uracil-DNA Glycosylase==
-
<StructureSection load='1oe6' size='340' side='right' caption='[[1oe6]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
+
<StructureSection load='1oe6' size='340' side='right'caption='[[1oe6]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1oe6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OE6 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1oe6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OE6 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HMU:5-HYDROXYMETHYL+URACIL'>HMU</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HMU:5-HYDROXYMETHYL+URACIL'>HMU</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oe4|1oe4]], [[1oe5|1oe5]]</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=1oe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe6 OCA], [https://pdbe.org/1oe6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oe6 RCSB], [https://www.ebi.ac.uk/pdbsum/1oe6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oe6 ProSAT]</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=1oe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe6 OCA], [http://pdbe.org/1oe6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oe6 RCSB], [http://www.ebi.ac.uk/pdbsum/1oe6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oe6 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/SMUG1_XENLA SMUG1_XENLA]] Responsible for recognizing base lesions in the genome and initiating base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has a preference for single-stranded DNA substrates. No enzymatic activity towards G/T mismatches.
+
[https://www.uniprot.org/uniprot/SMUG1_XENLA SMUG1_XENLA] Responsible for recognizing base lesions in the genome and initiating base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has a preference for single-stranded DNA substrates. No enzymatic activity towards G/T mismatches.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 21: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oe6 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oe6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
Cytosine deamination is a major promutagenic process, generating G:U mismatches that can cause transition mutations if not repaired. Uracil is also introduced into DNA via nonmutagenic incorporation of dUTP during replication. In bacteria, uracil is excised by uracil-DNA glycosylases (UDG) related to E. coli UNG, and UNG homologs are found in mammals and viruses. Ung knockout mice display no increase in mutation frequency due to a second UDG activity, SMUG1, which is specialized for antimutational uracil excision in mammalian cells. Remarkably, SMUG1 also excises the oxidation-damage product 5-hydroxymethyluracil (HmU), but like UNG is inactive against thymine (5-methyluracil), a chemical substructure of HmU. We have solved the crystal structure of SMUG1 complexed with DNA and base-excision products. This structure indicates a more invasive interaction with dsDNA than observed with other UDGs and reveals an elegant water displacement/replacement mechanism that allows SMUG1 to exclude thymine from its active site while accepting HmU.
 
- 
-
Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1.,Wibley JE, Waters TR, Haushalter K, Verdine GL, Pearl LH Mol Cell. 2003 Jun;11(6):1647-59. PMID:12820976<ref>PMID:12820976</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1oe6" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
-
*[[DNA glycosylase|DNA glycosylase]]
+
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: African clawed frog]]
+
[[Category: Large Structures]]
-
[[Category: Pearl, L H]]
+
[[Category: Xenopus laevis]]
-
[[Category: Wibley, J E.A]]
+
[[Category: Pearl LH]]
-
[[Category: Dna glycosylase]]
+
[[Category: Wibley JEA]]
-
[[Category: Hydrolase]]
+
-
[[Category: Hydrolase-dna complex]]
+
-
[[Category: Single stranded]]
+

Current revision

Xenopus SMUG1, an anti-mutator uracil-DNA Glycosylase

PDB ID 1oe6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools