1ODF
Structure of YGR205w protein.
Summary for 1ODF
| Entry DOI | 10.2210/pdb1odf/pdb |
| Descriptor | HYPOTHETICAL 33.3 KDA PROTEIN IN ADE3-SER2 INTERGENIC REGION, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | yeast protein, atp binding protein |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Cytoplasm: P42938 |
| Total number of polymer chains | 1 |
| Total formula weight | 33841.15 |
| Authors | Li De La Sierra-Gallay, I.,Van Tilbeurgh, H. (deposition date: 2003-02-19, release date: 2003-12-12, Last modification date: 2024-05-08) |
| Primary citation | Li De La Sierra-Gallay, I.,Collinet, B.,Graille, M.,Quevillon-Cheruel, S.,Liger, D.,Minard, P.,Blondeau, K.,Henckes, G.,Aufrere, R.,Leulliot, N.,Zhou, C.Z.,Sorrel, I.,Ferrer, J.L.,Poupon, A.,Janin, J.,Van Tilbeurgh, H. Crystal Structure of the Ygr205W Protein from Saccharomyces Cerevisiae: Close Structural Resemblance to E.Coli Pantothenate Kinase Proteins: Struct.,Funct., Genet., 54:776-, 2004 Cited by PubMed Abstract: 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. PubMed: 14997573DOI: 10.1002/PROT.10596 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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