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Crystal structure of a putative CN hydrolase from yeast
Author(s) -
Kumaran Desigan,
Eswaramoorthy Subramaniam,
Gerchman Sue Ellen,
Kycia Helen,
Studier F. William,
Swaminathan Subramanyam
Publication year - 2003
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.10417
Subject(s) - hydrolase , structural genomics , active site , crystal structure , dimer , yeast , chemistry , sequence alignment , sequence (biology) , cysteine , multiple isomorphous replacement , protein structure , crystallography , serine , structural similarity , serine hydrolase , peptide sequence , stereochemistry , protein crystallization , biochemistry , enzyme , gene , organic chemistry , crystallization
The crystal structure of a yeast hypothetical protein with sequence similarity to CN hydrolases has been determined to 2.4 Å resolution by the multiwavelength anomalous dispersion (MAD) method. The protein folds as a four‐layer αββα sandwich and exists as a dimer in the crystal and in solution. It was selected in a structural genomics project as representative of CN hydrolases at a time when no structures had been determined for members of this family. Structures for two other members of the family have since been reported and the three proteins have similar topology and dimerization modes, which are distinct from those of other αββα proteins whose structures are known. The dimers form an unusual eight‐layer αββα:αββα structure. Although the precise enzymatic reactions catalyzed by the yeast protein are not known, considerable information about the active site may be deduced from conserved sequence motifs, comparative biochemical information, and comparison with known structures of hydrolase active sites. As with serine hydrolases, the active‐site nucleophile (cysteine in this case) is positioned on a nucleophile elbow. Proteins 2003;52:283–291. © 2003 Wiley‐Liss, Inc.