1XE8: Crystal Structure Of The Yml079w Protein From Saccharomyces Cerevisiae Reveals A New Sequence Family Of The Jelly Roll Fold

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.
PDB ID: 1XE8Download
MMDB ID: 31437
PDB Deposition Date: 2004/9/9
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 1XE8: dimeric; determined by author and by software (PISA)
Molecular Components in 1XE8
Label Count Molecule
Proteins (2 molecules)
Hypothetical 22.5 KDA Protein in Tub1-cpr3 Intergenic Region(Gene symbol: YML079W)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB