3RQ5
Crystal Structure of ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Bacillus subtilis co-crystallized with ATP/Mg2+ and soaked with CoA
Summary for 3RQ5
| Entry DOI | 10.2210/pdb3rq5/pdb |
| Related | 1KYH 3RPZ 3RQ6 3RQ8 3RQH 3RQQ 3RQX |
| Descriptor | ADP/ATP-dependent NAD(P)H-hydrate dehydratase, COENZYME A, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | structural genomics, psi-biology, protein structure initiative, midwest center for structural genomics, mcsg, lyase, lyase-lyase substrate complex, lyase/lyase substrate |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 31128.16 |
| Authors | Shumilin, I.A.,Cymborowski, M.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2011-04-27, 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 Cited by 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: 22940582DOI: 10.1016/j.str.2012.07.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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