PDBsum entry 2q0x

Structural genomics, unknown function

PDB id: 2q0x

Contents

Protein chains

294 a.a. *

Ligands

GOL ×2

Waters ×123

* Residue conservation analysis

PDB id:

2q0x

Name:

Structural genomics, unknown function

Title:

Alpha/beta hydrolase fold protein of unknown function

Structure:

Uncharacterized protein. Chain: a, b. Synonym: protein duf1749. Engineered: yes

Source:

Trypanosoma brucei. Organism_taxid: 5691. Strain: treu927, 927/4 gutat10.1. Gene: tb10.6k15.0140. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.208 R-free: 0.250

Authors:

E.A.Merritt,Structural Genomics Of Pathogenic Protozoa Consortium (Sgpp)

Key ref:

E.A.Merritt et al. (2008). Structure of a Trypanosoma brucei alpha/beta-hydrolase fold protein with unknown function. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 474-478. PubMed id: 18540054

Date:

22-May-07 Release date: 26-Jun-07

Protein chains

Q389W3  (Q389W3_TRYB2) -  Paraflagellar rod component from Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

Seq: 331 a.a.

Struc: 294 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Acta Crystallogr Sect F Struct Biol Cryst Commun 64:474-478 (2008)

PubMed id: 18540054

Structure of a Trypanosoma brucei alpha/beta-hydrolase fold protein with unknown function.

E.A.Merritt, M.Holmes, F.S.Buckner, W.C.Van Voorhis, E.Quartly, E.M.Phizicky, A.Lauricella, J.Luft, G.DeTitta, H.Neely, F.Zucker, W.G.Hol.

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.