3RSG
Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima soaked with NAD.
Summary for 3RSG
| Entry DOI | 10.2210/pdb3rsg/pdb |
| Related | 2AX3 3RNO 3RO7 3ROE 3ROG 3ROX 3ROZ 3RRB 3RRE 3RRF 3RRJ 3RS8 3RS9 3RSF 3RSQ 3RSS 3RT7 3RT9 3RTA 3RTB 3RTC 3RTD 3RTE 3RTG 3RU2 3RU3 |
| Descriptor | Putative uncharacterized protein, Unknown peptide, probably from expression host, POTASSIUM ION, ... (7 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 | 57213.01 |
| Authors | Shumilin, I.A.,Cymborowski, M.,Lesley, S.A.,Minor, W. (deposition date: 2011-05-02, 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 (2.1 Å) |
Structure validation
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