Motion in Trp RNA-binding attenuation protein [trprbatten]

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Classification Suspected Domain Motion, Hinge Mechanism [D-h-1]

Structures 1QAW 1WAP With tryptophan [ PartsList ]

Description Trp RNA-binding attenuation protein's eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel structure with a large central hole. The nature of binding of L-tryptophan in the clefts between adjacent beta-sheets in the beta-wheel suggested to Antson et al. (1995) that this binding induces conformation changes in the flexible residues 25-33 and 49-52 (presumably hinges). To date (Sept 1997) only one crystal structure has been solved.

Particular values describing motion Creation Date = 19970822 Modification Date = 19970822 Location of a Hinge (residue selection) = 25-33 (core region hinge 1?) Location of a Hinge (residue selection) = 49-52 (core region hinge 2?) Experimental Methods = x (Traditional x-ray)

References A A Antson, J Otridge, A M Brzozowski, E J Dodson, G G Dodson, K S Wilson, T M Smith, M Yang, T Kurecki, and P Gollnick (1995). The structure of trp RNA-binding attenuation protein. Nat. 374:693-700. [Medline info for 7715723]

GO terms associated with structures Molecular function RNA binding Biological process regulation of transcription, DNA-dependent, transcription termination

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu