3RQ5: Crystal Structure Of AdpATP-Dependent Nad(P)h-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized With AtpMG2+ AND SOAKED WITH Coa

Citation:
Abstract
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: 3RQ5Download
MMDB ID: 93191
PDB Deposition Date: 2011/4/27
Updated in MMDB: 2011/09
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3RQ5: tetrameric; determined by author and by software (PISA)
Molecular Components in 3RQ5
Label Count Molecule
Proteins (4 molecules)
4
Adp/atp-dependent Nad(p)h-hydrate Dehydratase(Gene symbol: yxkO)
Molecule annotation
Chemicals (12 molecules)
1
4
2
8
* Click molecule labels to explore molecular sequence information.

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