Motion in Diphtheria Toxin (DT) [dt]

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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

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Diptheria Toxin (slo 1ddt [ A ] 1mdt [ A ] 535

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
dt 1ddt [ ] 1mdt [ ] 535
910970-7569 Diphtheria Toxin Repressor 1bi0 [ A ] 1bi3 [ A ] 225
911955-9329 Diphtheria Toxin Repressor 1bi2 [ A ] 1bi3 [ A ] 225
911915-9306 Diphtheria Toxin Repressor 1bi0 [ A ] 1bi2 [ A ] 226
911983-9351 Diphtheria Toxin Repressor 1bi1 [ A ] 1bi3 [ A ] 225
85736-19136 Diptheria Toxin (DT) 1ddt [ A ] 1mdt [ A ] 535


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