Structural highlights
4qvb is a 2 chain structure with sequence from Mycobacterium tuberculosis 7199-99. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Method: | X-ray diffraction, Resolution 2.3Å |
Ligands: | , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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]
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