Crystal structure of the YGR205w protein from Saccharomyces cerevisiae: Close structural resemblance to E. coli pantothenate kinase

• Published in: Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2004-03, Vol.54 (4), p.776-783
• Main Authors: Li de La Sierra-Gallay, Ines, Collinet, Bruno, Graille, Marc, Quevillon-Cheruel, Sophie, Liger, Dominique, Minard, Philippe, Blondeau, Karine, Henckes, Gilles, Aufrère, Robert, Leulliot, Nicolas, Zhou, Cong-Zhao, Sorel, Isabelle, Ferrer, Jean-Luc, Poupon, Anne, Janin, Joël, van Tilbeurgh, Herman
• Format: Article
• Language: English
• Subjects: Adenosine Diphosphate - metabolism; Adenosine Triphosphate - metabolism; Amino Acid Sequence; Binding Sites; Biochemistry, Molecular Biology; crystal structure; Crystallization; Crystallography, X-Ray; Escherichia coli - enzymology; kinase; Life Sciences; Microbiology and Parasitology; Molecular Sequence Data; mononucleotide binding fold; Mycology; nucleotide; P-loop; Phosphotransferases (Alcohol Group Acceptor) - chemistry; Saccharomyces cerevisiae - chemistry; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Structural Biology; structural genomics; Substrate Specificity; Sulfates - metabolism; yeast; YGR205w
• ISSN: 0887-3585; 1097-0134
• DOI: 10.1002/prot.10596

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 β‐phosphate in mononucleotide protein ATP complex, suggesting the protein is indeed a kinase. The nature of the phosphate accepting substrate remains to be determined. Proteins 2004;54:000–000. © 2004 Wiley‐Liss, Inc.