Structural highlights
Function
[SP0F_BACSU] Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.
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
As a part of studies on the structural characterization of the components of the sporulation phosphorelay in Bacillus subtilis, the crystal structure of the manganese derivative of an intermediate signal transducer, Spo0F, has been elucidated at 2.25 A resolution. The calcium complex and the apo structures have been analyzed previously. In apo Spo0F, the active-site cation cavity is only partially formed and it only becomes completed upon metal coordination. The carbonyl of Lys56 is coordinated to the metal and interestingly the side chain of Lys56 exists in a variety of conformations in the three crystal structures of Spo0F. The affinity of the magnesium ion for Spo0F is in fact low; however, it binds Spo0F when it is in complex with Spo0B. It is proposed that the existence of a deep pocket which extends from the surface to the metal site could attract and direct the metal, thereby facilitating the metal binding of the complex.
Metals in the sporulation phosphorelay: manganese binding by the response regulator Spo0F.,Mukhopadhyay D, Sen U, Zapf J, Varughese KI Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):638-45. Epub 2004, Mar 23. PMID:15039551[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mukhopadhyay D, Sen U, Zapf J, Varughese KI. Metals in the sporulation phosphorelay: manganese binding by the response regulator Spo0F. Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):638-45. Epub 2004, Mar 23. PMID:15039551 doi:10.1107/S0907444904002148