3RS9: Crystal Structure Of Tm0922, A Fusion Of A Domain Of Unknown Function And AdpATP-Dependent Nad(P)h-Hydrate Dehydratase From Thermotoga Maritima In Complex With P1,P3-Di(Adenosine-5') Triphosphate

Proteins of unknown function comprise a significant fraction of sequenced genomes. Defining the roles of these proteins is vital to understanding cellular processes. Here, we describe a method to determine a protein function based on the identification of its natural ligand(s) by the crystallographic screening of the binding of a metabolite library, followed by a focused search in the metabolic space. The method was applied to two protein families with unknown function, PF01256 and YjeF_N. The PF01256 proteins, represented by YxkO from Bacillus subtilis and the C-terminal domain of Tm0922 from Thermotoga maritima, were shown to catalyze ADP/ATP-dependent NAD(P)H-hydrate dehydratation, a previously described orphan activity. The YjeF_N proteins, represented by mouse apolipoprotein A-I binding protein and the N-terminal domain of Tm0922, were found to interact with an adenosine diphosphoribose-related substrate and likely serve as ADP-ribosyltransferases. Crystallographic screening of metabolites serves as an efficient tool in functional analyses of uncharacterized proteins.
PDB ID: 3RS9Download
MMDB ID: 91963
PDB Deposition Date: 2011/5/2
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Escherichia coli BL21(DE3)
Similar Structures:
Biological Unit for 3RS9: hexadecameric; determined by author and by software (PISA)
Molecular Components in 3RS9
Label Count Molecule
Proteins (16 molecules)
Putative Uncharacterized Protein(Gene symbol: TM0922)
Molecule annotation
Unknown Peptide, Probably From Expression Host
Molecule annotation
Chemicals (40 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB