Structural rearrangement accompanying ligand binding in the GAF domain of CodY from Bacillus subtilis.

ABSTRACT: The GAF domain is a simple module widespread in proteins of diverse function, including cell signalling proteins and transcription factors. Its structure, typically spanning 150 residues, has three tiers: a basal layer of two or more alpha-helices, a middle layer of beta-pleated sheet and a top layer formed by segments of the polypeptide that connect strands of the beta-sheet. In structures of GAF domains in complex with their effectors, these polypeptide segments envelop the ligand, enclosing it in a cavity whose base is formed by the beta-sheet, such that ligand binding and release must be accompanied by conformational rearrangements of the distal portion of the structure. Descriptions of binding are presently limited by the absence of a GAF domain for which both liganded and unliganded

SUBMITTER: Levdikov VM 

PROVIDER: S-EPMC3128921 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature