View source for 4wpk


==Crystal structure of Mycobacterium tuberculosis uracil-DNA glycosylase, Form I==
<StructureSection load='4wpk' size='340' side='right'caption='[[4wpk]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WPK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=4wpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wpk OCA], [https://pdbe.org/4wpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wpk RCSB], [https://www.ebi.ac.uk/pdbsum/4wpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wpk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UNG_MYCTU UNG_MYCTU] 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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
17 independent crystal structures of family I uracil-DNA glycosylase from Mycobacterium tuberculosis (MtUng) and its complexes with uracil and its derivatives, distributed among five distinct crystal forms, have been determined. Thermodynamic parameters of binding in the complexes have been measured using isothermal titration calorimetry. The two-domain protein exhibits open and closed conformations, suggesting that the closure of the domain on DNA binding involves conformational selection. Segmental mobility in the enzyme molecule is confined to a 32-residue stretch which plays a major role in DNA binding. Uracil and its derivatives can bind to the protein in two possible orientations. Only one of them is possible when there is a bulky substituent at the 5' position. The crystal structures of the complexes provide a reasonable rationale for the observed thermodynamic parameters. In addition to providing fresh insights into the structure, plasticity and interactions of the protein molecule, the results of the present investigation provide a platform for structure-based inhibitor design.

Structural plasticity in Mycobacterium tuberculosis uracil-DNA glycosylase (MtUng) and its functional implications.,Arif SM, Geethanandan K, Mishra P, Surolia A, Varshney U, Vijayan M Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1514-27. doi:, 10.1107/S1399004715009311. Epub 2015 Jun 30. PMID:26143923<ref>PMID:26143923</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4wpk" style="background-color:#fffaf0;"></div>

==See Also==
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Arif SM]]
[[Category: Geethanandan K]]
[[Category: Mishra P]]
[[Category: Surolia A]]
[[Category: Varshney U]]
[[Category: Vijayan M]]