View source for 1wpi


==Solution NMR Structure of Protein YKR049C from Saccharomyces cerevisiae. Ontario Centre for Structural Proteomics target YST0250_1_133; Northeast Structural Genomics Consortium YTYst250==
<StructureSection load='1wpi' size='340' side='right'caption='[[1wpi]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wpi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WPI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1wpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpi OCA], [https://pdbe.org/1wpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wpi RCSB], [https://www.ebi.ac.uk/pdbsum/1wpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wpi ProSAT], [https://www.topsan.org/Proteins/NESGC/1wpi TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FMP46_YEAST FMP46_YEAST] Putative mitochondrial redox protein which could be involved in the reduction of small toxic molecules.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
YKR049C is a mitochondrial protein in Saccharomyces cerevisiae that is conserved among yeast species, including Candida albicans. However, no biological function for YKR049C has been ascribed based on its primary sequence information. In the present study, NMR spectroscopy was used to determine the putative biological function of YKR049C based on its solution structure. YKR049C shows a well-defined thioredoxin fold with a unique insertion of helices between two beta-strands. The central beta-sheet divides the protein into two parts; a unique face and a conserved face. The 'unique face' is located between beta2 and beta3. Interestingly, the sequences most conserved among YKR049C families are found on this 'unique face', which incorporates L109 to E114. The side chains of these conserved residues interact with residues on the helical region with a stretch of hydrophobic surface. A putative active site composed by two short helices and a single Cys97 was also well observed. Our findings suggest that YKR049C is a redox protein with a thioredoxin fold containing a single active cysteine.

Solution structure of YKR049C, a putative redox protein from Saccharomyces cerevisiae.,Jung JW, Yee A, Wu B, Arrowsmith CH, Lee W J Biochem Mol Biol. 2005 Sep 30;38(5):550-4. PMID:16202234<ref>PMID:16202234</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1wpi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Arrowsmith CH]]
[[Category: Jung JW]]
[[Category: Lee W]]
[[Category: Yee A]]