1XE8

Crystal structure of the YML079w protein from Saccharomyces cerevisiae reveals a new sequence family of the jelly roll fold.

Summary for 1XE8

• Entry DOI: 10.2210/pdb1xe8/pdb
• Related: 1XE7
• Descriptor: Hypothetical 22.5 kDa protein in TUB1-CPR3 intergenic region, ADENINE, CITRIC ACID, ... (5 entities in total)
• Functional Keywords: jelly roll motif, cupin superfamily, structural genomics, yml079wp, s. cerevisiae, unknown function
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 3
• Total formula weight: 69126.53

Authors

Zhou, C.-Z.,Meyer, P.,Quevillon-Cheruel, S.,Li de La Sierra-Gallay, I.,Collinet, B.,Graille, M.,Leulliot, N.,Sorel, I.,Janin, J.,Van Tilbeurgh, H. (deposition date: 2004-09-09, release date: 2005-01-11, Last modification date: 2024-11-13)

Primary citation

Zhou, C.-Z.,Meyer, P.,Quevillon-Cheruel, S.,Li de La Sierra-Gallay, I.,Collinet, B.,Graille, M.,Blondeau, K.,Leulliot, N.,Sorel, I.,Poupon, A.,Janin, J.,Van Tilbeurgh, H.
Crystal structure of the YML079w protein from Saccharomyces cerevisiae reveals a new sequence family of the jelly-roll fold
Protein Sci., 14:209-215, 2005

PubMed Abstract: 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 A. 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 beta-strands organized in two parallel packed beta-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 beta-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.

PubMed: 15608122
DOI: 10.1110/ps.041121305

Experimental method

X-RAY DIFFRACTION (2.8 Å)