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Crystal structure of the YGR205w protein from Saccharomyces cerevisiae : Close structural resemblance to E. coli pantothenate kinase
Author(s) -
Li de La SierraGallay Ines,
Collinet Bruno,
Graille Marc,
QuevillonCheruel Sophie,
Liger Dominique,
Minard Philippe,
Blondeau Karine,
Henckes Gilles,
Aufrère Robert,
Leulliot Nicolas,
Zhou CongZhao,
Sorel Isabelle,
Ferrer JeanLuc,
Poupon Anne,
Janin Joël,
van Tilbeurgh Herman
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10596
Subject(s) - structural genomics , saccharomyces cerevisiae , biochemistry , protein structure , active site , biology , yeast , chemistry , enzyme
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.