1odf
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STRUCTURE OF YGR205W PROTEIN.
OverviewOverview
The protein product of the YGR205w gene of Saccharomyces cerevisiae was, targeted as part of our yeast structural genomics project. YGR205w codes, for a small (290 amino acids) protein with unknown structure and function., The only recognizable sequence feature is the presence of a Walker A motif, (P loop) indicating a possible nucleotide binding/converting function. We, determined the three-dimensional crystal structure of Se-methionine, substituted protein using multiple anomalous diffraction. The structure, revealed a well known mononucleotide fold and strong resemblance to the, structure of small metabolite phosphorylating enzymes such as pantothenate, and phosphoribulo kinase. Biochemical experiments show that YGR205w binds, specifically ATP and, less tightly, ADP. The structure also revealed the, presence of two bound sulphate ions, occupying opposite niches in a canyon, that corresponds to the active site of the protein. One sulphate is bound, to the P-loop in a position that corresponds to the position of, beta-phosphate in mononucleotide protein ATP complex, suggesting the, protein is indeed a kinase. The nature of the phosphate accepting, substrate remains to be determined.
About this StructureAbout this Structure
1ODF is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 and GOL as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the YGR205w protein from Saccharomyces cerevisiae: close structural resemblance to E. coli pantothenate kinase., de La Sierra-Gallay IL, Collinet B, Graille M, Quevillon-Cheruel S, Liger D, Minard P, Blondeau K, Henckes G, Aufrere R, Leulliot N, Zhou CZ, Sorel I, Ferrer JL, Poupon A, Janin J, van Tilbeurgh H, Proteins. 2004 Mar 1;54(4):776-83. PMID:14997573
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