4xeg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:44, 27 September 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Structure of the enzyme-product complex resulting from TDG action on a G/hmU mismatch==
==Structure of the enzyme-product complex resulting from TDG action on a G/hmU mismatch==
-
<StructureSection load='4xeg' size='340' side='right' caption='[[4xeg]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
+
<StructureSection load='4xeg' size='340' side='right'caption='[[4xeg]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4xeg]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XEG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XEG FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4xeg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XEG FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ORP:2-DEOXY-5-PHOSPHONO-RIBOSE'>ORP</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]] 1.72&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymine-DNA_glycosylase Thymine-DNA glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.29 3.2.2.29] </span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ORP:2-DEOXY-5-PHOSPHONO-RIBOSE'>ORP</scene></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=4xeg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xeg OCA], [http://pdbe.org/4xeg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xeg RCSB], [http://www.ebi.ac.uk/pdbsum/4xeg PDBsum]</span></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=4xeg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xeg OCA], [https://pdbe.org/4xeg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xeg RCSB], [https://www.ebi.ac.uk/pdbsum/4xeg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xeg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/TDG_HUMAN TDG_HUMAN]] In the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. This enzyme corrects G/T mispairs to G/C pairs. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine.
+
[https://www.uniprot.org/uniprot/TDG_HUMAN TDG_HUMAN] In the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. This enzyme corrects G/T mispairs to G/C pairs. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 18: Line 19:
</div>
</div>
<div class="pdbe-citations 4xeg" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4xeg" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Thymine-DNA glycosylase]]
+
[[Category: Homo sapiens]]
-
[[Category: Drohat, A C]]
+
[[Category: Large Structures]]
-
[[Category: Malik, S S]]
+
[[Category: Unidentified]]
-
[[Category: Pozharski, E]]
+
[[Category: Drohat AC]]
-
[[Category: 5-hydroxymethyluracil]]
+
[[Category: Malik SS]]
-
[[Category: Abasic site]]
+
[[Category: Pozharski E]]
-
[[Category: Dna glycosylase]]
+
-
[[Category: Enzyme-product complex]]
+
-
[[Category: Hydrolase-dna complex]]
+

Current revision

Structure of the enzyme-product complex resulting from TDG action on a G/hmU mismatch

PDB ID 4xeg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xeg"
Personal tools