3RQQ: Crystal Structure Of AdpATP-Dependent Nad(P)h-Hydrate Dehydratase From Bacillus Subtilis 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: 3RQQDownload
MMDB ID: 93195
PDB Deposition Date: 2011/4/28
Updated in MMDB: 2011/09
Experimental Method:
x-ray diffraction
Resolution: 1.6  Å
Source Organism:
Similar Structures:
Biological Unit for 3RQQ: tetrameric; determined by author and by software (PISA)
Molecular Components in 3RQQ
Label Count Molecule
Proteins (4 molecules)
Adp/atp-dependent Nad(p)h-hydrate Dehydratase(Gene symbol: yxkO)
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB