Motion in Diphtheria Toxin (DT) [dt]

[ jump to morphs ]

Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures
1DDT Conformation 1 [ PartsList ]
1MDT Conformation 2 [ PartsList ]

Description
1 interdomain linkage, 1 hinge, 180 degree rotation, motions up to 65 A. Comparison of monomer and dimer reveal one domain has moved to a more open conformation in the latter.

Particular values describing motion
Experimental Methods = x (Traditional x-ray)
Modification Date = 1999-08-14 17:02:13.000
Creation Date = 19970822

References
M J Bennett, M P Schlunegger, and D Eisenberg (1995). 3D Domain swapping: A Mechanism for oligomer assembly. Prot. Sci 4:2455-2468. [Medline info for 96164377]
M J Bennett, S Choe and D Eisenberg (1994). Domain swapping: entangling alliances between proteins. Proc Natl Acad Sci U S A. 91: 3127-3131. [Medline info for 94211815]

GO terms associated with structures
Molecular functionNAD+-diphthamide ADP-ribosyltransferase activity
Cellular componentextracellular region
Biological processpathogenesis

Morphs

[ show all images ]
Best representative
Morph Morph name Structure #1 Structure #2 Residues
[ ] [ ]



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