Structural highlights
Function
MOBB_ECOLI GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Eaves DJ, Palmer T, Boxer DH. The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein. Eur J Biochem. 1997 Jun 15;246(3):690-7. PMID:9219527
- ↑ Temple CA, Rajagopalan KV. Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J Biol Chem. 2000 Dec 22;275(51):40202-10. PMID:10978348 doi:http://dx.doi.org/10.1074/jbc.M007407200
- ↑ McLuskey K, Harrison JA, Schuttelkopf AW, Boxer DH, Hunter WN. Insight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structure. J Biol Chem. 2003 Jun 27;278(26):23706-13. Epub 2003 Apr 7. PMID:12682065 doi:10.1074/jbc.M301485200
