3RRJ

Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima in complex with P1,P5-Di(adenosine-5') pentaphosphate

Summary for 3RRJ

• Entry DOI: 10.2210/pdb3rrj/pdb
• Related: 2AX3
• Descriptor: Bifunctional NAD(P)H-hydrate repair enzyme Nnr, peptide, POTASSIUM ION, ... (6 entities in total)
• Functional Keywords: unknown function, adp/atp-dependent nad(p)h-hydrate dehydratase, lyase
• Biological source: Thermotoga maritima; More
• Total number of polymer chains: 2
• Total formula weight: 56311.00

Authors

Shumilin, I.A.,Cymborowski, M.,Lesley, S.A.,Minor, W. (deposition date: 2011-04-29, release date: 2011-07-27, Last modification date: 2023-09-13)

Primary citation

Shumilin, I.A.,Cymborowski, M.,Chertihin, O.,Jha, K.N.,Herr, J.C.,Lesley, S.A.,Joachimiak, A.,Minor, W.
Identification of unknown protein function using metabolite cocktail screening.
Structure, 20:1715-1725, 2012

PubMed 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.

PubMed: 22940582
DOI: 10.1016/j.str.2012.07.016

Experimental method

X-RAY DIFFRACTION (2.5 Å)