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Crystal structure of the YML079w protein from Saccharomyces cerevisiae reveals a new sequence family of the jelly‐roll fold
Author(s) -
Zhou CongZhao,
Meyer Philippe,
QuevillonCheruel Sophie,
De La SierraGallay Inès Li,
Collinet Bruno,
Graille Marc,
Blondeau Karine,
François JeanMarie,
Leulliot Nicolas,
Sorel Isabelle,
Poupon Anne,
Janin Joel,
Van Tilbeurgh Herman
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.041121305
Subject(s) - saccharomyces cerevisiae , open reading frame , dimer , protein structure , biochemistry , structural similarity , yeast , protein family , chemistry , structural genomics , peptide sequence , biology , gene , organic chemistry
We determined the three‐dimensional crystal structure of the protein YML079wp, encoded by a hypothetical open reading frame from Saccharomyces cerevisiae to a resolution of 1.75 Å. The protein has no close homologs and its molecular and cellular functions are unknown. The structure of the protein is a jelly‐roll fold consisting of ten β‐strands organized in two parallel packed β‐sheets. The protein has strong structural resemblance to the plant storage and ligand binding proteins (canavalin, glycinin, auxin binding protein) but also to some plant and bacterial enzymes (epimerase, germin). The protein forms homodimers in the crystal, confirming measurements of its molecular mass in solution. Two monomers have their β‐sheet packed together to form the dimer. The presence of a hydrophobic ligand in a well conserved pocket inside the barrel and local sequence similarity with bacterial epimerases may suggest a biochemical function for this protein.