1ODF

Structure of YGR205w protein.

1ODF の概要

• エントリーDOI: 10.2210/pdb1odf/pdb
• 分子名称: HYPOTHETICAL 33.3 KDA PROTEIN IN ADE3-SER2 INTERGENIC REGION, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: yeast protein, atp binding protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Cytoplasm: P42938
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33841.15

構造登録者

Li De La Sierra-Gallay, I.,Van Tilbeurgh, H. (登録日: 2003-02-19, 公開日: 2003-12-12, 最終更新日: 2024-05-08)

主引用文献

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

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: 14997573
DOI: 10.1002/PROT.10596

実験手法

X-RAY DIFFRACTION (2.25 Å)