View source for 5uiv


==Structure of Thymidylate Kinase from Candida albicans Reveals Origin of Broad Substrate Specificity and a Novel Structural Element.==
<StructureSection load='5uiv' size='340' side='right'caption='[[5uiv]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5uiv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_SC5314 Candida albicans SC5314]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UIV 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]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</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=5uiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uiv OCA], [https://pdbe.org/5uiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uiv RCSB], [https://www.ebi.ac.uk/pdbsum/5uiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uiv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q59TV7_CANAL Q59TV7_CANAL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of thymidylate kinase from Candida albicans, determined by X-ray crystallography, is reported to a resolution of 2.45 A with a final Rfree of 0.223. Thymidylate kinase from C. albicans possesses a unique 15 residue loop that is not seen in thymidylate kinases from other genera. The structure reported here reveals that the conformation of this loop is constrained by both intra- and inter-subunit hydrogen bonding and a number of key residues in this loop are conserved among different Candida species of medical importance. The substrate specificity of the enzyme was determined using a novel NMR based assay as well as a traditional coupled assay. The enzyme is active against 3'-azido-3'-deoxythymidine (AZT) and moderately active with dGMP. The distinct functional and structural differences between the C. albicans enzyme and the human enzyme suggest that thymidylate kinase is an appropriate target for the development of new anti-fungal agents.

Structure of Thymidylate Kinase from Candida albicans Reveals a Unique Structural Element.,Sinha K, Rule GS Biochemistry. 2017 Jul 25. doi: 10.1021/acs.biochem.7b00498. PMID:28742342<ref>PMID:28742342</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5uiv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candida albicans SC5314]]
[[Category: Large Structures]]
[[Category: Rule GS]]
[[Category: Sinha K]]