Structural highlights
Function
MODA_XANAC Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (Probable). Binds molybdate and tungstate with high affinity in vitro (PubMed:16879982).[1]
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
Xanthomonas axonopodis pv. citri ModA protein is the ABC periplasmic binding component responsible for the capture of molybdate. The protein was crystallized with sodium molybdate using the hanging-drop vapour-diffusion method in the presence of PEG or sulfate. X-ray diffraction data were collected to a maximum resolution of 1.7 A using synchrotron radiation. The crystal belongs to the orthorhombic space group C222(1), with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 A. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.
Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri.,Santacruz CP, Balan A, Ferreira LC, Barbosa JA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt, 3):289-91. Epub 2006 Feb 24. PMID:16511325[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Balan A, Santacruz CP, Moutran A, Ferreira RC, Medrano FJ, Pérez CA, Ramos CH, Ferreira LC. The molybdate-binding protein (ModA) of the plant pathogen Xanthomonas axonopodis pv. citri. Protein Expr Purif. 2006 Dec;50(2):215-22. PMID:16879982 doi:10.1016/j.pep.2006.06.014
- ↑ Santacruz CP, Balan A, Ferreira LC, Barbosa JA. Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt, 3):289-91. Epub 2006 Feb 24. PMID:16511325 doi:10.1107/S1744309106003812
