3rox: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>  
[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>  
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== Publication Abstract from PubMed ==
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.
Identification of Unknown Protein Function Using Metabolite Cocktail Screening.,Shumilin IA, Cymborowski M, Chertihin O, Jha KN, Herr JC, Lesley SA, Joachimiak A, Minor W Structure. 2012 Aug 28. PMID:22940582<ref>PMID:22940582</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
<references/>
<references/>

Revision as of 15:32, 14 March 2024

Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with TheophyllineCrystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline

Structural highlights

3rox is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NNRE_MOUSE Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159][1]

References

  1. ↑ Marbaix AY, Noel G, Detroux AM, Vertommen D, Van Schaftingen E, Linster CL. Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair. J Biol Chem. 2011 Dec 2;286(48):41246-52. doi: 10.1074/jbc.C111.310847. Epub 2011, Oct 12. PMID:21994945 doi:http://dx.doi.org/10.1074/jbc.C111.310847

3rox, resolution 2.40Å

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OCA
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