2Q0X

Alpha/Beta hydrolase fold protein of unknown function

Summary for 2Q0X

• Entry DOI: 10.2210/pdb2q0x/pdb
• Descriptor: Uncharacterized protein, GLYCEROL (3 entities in total)
• Functional Keywords: alpha/beta hydrolase fold, structural genomics, structural genomics of pathogenic protozoa consortium, sgpp, psi, protein structure initiative, unknown function
• Biological source: Trypanosoma brucei
• Total number of polymer chains: 2
• Total formula weight: 74902.82

Authors

Merritt, E.A.,Structural Genomics of Pathogenic Protozoa Consortium (SGPP) (deposition date: 2007-05-22, release date: 2007-06-26, Last modification date: 2024-02-21)

Primary citation

Merritt, E.A.,Holmes, M.,Buckner, F.S.,Van Voorhis, W.C.,Quartly, E.,Phizicky, E.M.,Lauricella, A.,Luft, J.,DeTitta, G.,Neely, H.,Zucker, F.,Hol, W.G.
Structure of a Trypanosoma brucei alpha/beta-hydrolase fold protein with unknown function.
Acta Crystallogr.,Sect.F, 64:474-478, 2008

PubMed Abstract: The structure of a structural genomics target protein, Tbru020260AAA from Trypanosoma brucei, has been determined to a resolution of 2.2 A using multiple-wavelength anomalous diffraction at the Se K edge. This protein belongs to Pfam sequence family PF08538 and is only distantly related to previously studied members of the alpha/beta-hydrolase fold family. Structural superposition onto representative alpha/beta-hydrolase fold proteins of known function indicates that a possible catalytic nucleophile, Ser116 in the T. brucei protein, lies at the expected location. However, the present structure and by extension the other trypanosomatid members of this sequence family have neither sequence nor structural similarity at the location of other active-site residues typical for proteins with this fold. Together with the presence of an additional domain between strands beta6 and beta7 that is conserved in trypanosomatid genomes, this suggests that the function of these homologs has diverged from other members of the fold family.

PubMed: 18540054
DOI: 10.1107/S174430910801141X

Experimental method

X-RAY DIFFRACTION (2.2 Å)