1ct5

<StructureSection load='1ct5' size='340' side='right'caption='[[1ct5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ct5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CT5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1ct5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ct5 OCA], [http://pdbe.org/1ct5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ct5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ct5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ct5 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1ct5 TOPSAN]</span></td></tr>

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== Publication Abstract from PubMed ==

Yeast hypothetical protein YBL036C (SWISS-PROT P38197), initially thought to be a member of an 11-protein family, was selected for crystal structure determination since no structural or functional information was available. The structure has been determined independently by MIR and MAD methods to 2.0 A resolution. The MAD structure was determined largely through automated model building. The protein folds as a TIM barrel beginning with a long N-terminal helix, in contrast to the classic triose phosphate isomerase (TIM) structure, which begins with a beta-strand. A cofactor, pyridoxal 5'-phosphate, is covalently bound near the C-terminal end of the barrel, the usual active site in TIM-barrel folds. A single-domain monomeric molecule, this yeast protein resembles the N-terminal domain of alanine racemase or ornithine decarboxylase, both of which are two-domain dimeric proteins. The yeast protein has been shown to have amino-acid racemase activity. Although selected as a member of a protein family having no obvious relationship to proteins of known structure, the protein fold turned out to be a well known and widely distributed fold. This points to the need for a more comprehensive base of structural information and better structure-modeling tools before the goal of structure prediction from amino-acid sequences can be realised. In this case, similarity to a known structure allowed inferences to be made about the structure and function of a widely distributed protein family.

Structure of a yeast hypothetical protein selected by a structural genomics approach.,Eswaramoorthy S, Gerchman S, Graziano V, Kycia H, Studier FW, Swaminathan S Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):127-35. Epub 2002, Dec 19. PMID:12499548<ref>PMID:12499548</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 1ct5" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Burley, S K]]

[[Category: Eswaramoorthy, S]]

[[Category: Structural genomic]]

[[Category: Swaminathan, S]]

[[Category: Yeast]]