1xe8

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spinqualitylabelsall models 1xe8, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1XE8 is a Single protein structure of sequence from Saccharomyces cerevisiae with ADE, CIT and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the YML079w protein from Saccharomyces cerevisiae reveals a new sequence family of the jelly-roll fold., Zhou CZ, Meyer P, Quevillon-Cheruel S, De La Sierra-Gallay IL, Collinet B, Graille M, Blondeau K, Francois JM, Leulliot N, Sorel I, Poupon A, Janin J, Van Tilbeurgh H, Protein Sci. 2005 Jan;14(1):209-15. PMID:15608122

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