Structural highlights
Function
F420R_MYCTU F420H(2)-dependent reductase able to catalyze the reduction of biliverdin-IXalpha to bilirubin-IXalpha in vitro. However, kinetic parameters show that it is less efficient than the biliverdin reductase Rv2074 and suggest biliverdin-IXalpha is unlikely to be the native substrate of Rv1155, which probably catalyzes the reduction of an alternative molecule in vivo (PubMed:27364382). Binds coenzyme F420, but does not bind FMN or other flavins (PubMed:25644473). Cannot use pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate, pyridoxal 5'-phosphate (PLP), the anti-tuberculosis drug PA-824 or aflatoxin analogs as substrates (PubMed:25644473).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
With the aim of elucidating the biological function of hypothetical proteins unique amongst the Actynomyces sub-group of bacteria, we have solved the crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis at 1.8 A resolution. Rv1155 is a homodimer both in the crystal structure and in solution and folds into two separate domains consisting of a six-stranded anti-parallel beta-barrel fold flanked by two alpha-helices and a helix-turn-helix domain. Both domains contribute to the formation of two deep clefts at the dimer interface. The overall fold of Rv1155 strikingly resembles that of flavin mononucleotide-binding protein and pyridoxamine 5'-phosphate oxydase, but the architecture of the putative binding pocket is markedly different, consistent with the lack of color of Rv1155 and its inability to bind FMN. Rv1155 thus appears to belong to a group of proteins with stringent conservation of the binding cleft, having evolved towards a new binding function.
Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis.,Canaan S, Sulzenbacher G, Roig-Zamboni V, Scappuccini-Calvo L, Frassinetti F, Maurin D, Cambillau C, Bourne Y FEBS Lett. 2005 Jan 3;579(1):215-21. PMID:15620716[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mashalidis EH, Gittis AG, Tomczak A, Abell C, Barry CE 3rd, Garboczi DN. Molecular insights into the binding of coenzyme F to the conserved protein Rv1155 from Mycobacterium tuberculosis. Protein Sci. 2015 Jan 31. doi: 10.1002/pro.2645. PMID:25644473 doi:http://dx.doi.org/10.1002/pro.2645
- ↑ Ahmed FH, Mohamed AE, Carr PD, Lee BM, Condic-Jurkic K, O'Mara ML, Jackson CJ. Rv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosis. Protein Sci. 2016 Jul 1. doi: 10.1002/pro.2975. PMID:27364382 doi:http://dx.doi.org/10.1002/pro.2975
- ↑ Canaan S, Sulzenbacher G, Roig-Zamboni V, Scappuccini-Calvo L, Frassinetti F, Maurin D, Cambillau C, Bourne Y. Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis. FEBS Lett. 2005 Jan 3;579(1):215-21. PMID:15620716 doi:10.1016/j.febslet.2004.11.069
