Abstract:
:A basis for understanding specificity of molecular recognition between phosphorelay proteins has been deduced from the 2.6 A structure of the Spo0B phosphotransferase of the phosphorelay regulating sporulation initiation. Spo0B consists of two domains: an N-terminal alpha-helical hairpin domain and a C-terminal alpha/beta domain. Two subunits of Spo0B dimerize by a parallel association of helical hairpins to form a novel four-helix bundle from which the active histidine protrudes. Docking studies show that both the monomers interact with a Spo0F molecule at the region surrounding the active site aspartate to position it for phosphotransfer. It is apparent that different surfaces of response regulators may be involved in recognition of the protein partners to which they are paired.
journal_name
Mol Celljournal_title
Molecular cellauthors
Varughese KI,Madhusudan,Zhou XZ,Whiteley JM,Hoch JAdoi
10.1016/s1097-2765(00)80148-3subject
Has Abstractpub_date
1998-10-01 00:00:00pages
485-93issue
4eissn
1097-2765issn
1097-4164pii
S1097-2765(00)80148-3journal_volume
2pub_type
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