Motion in G(i alpha 1) [gia1]

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Classification Known Domain Motion, Partial Refolding of Structure [D-f-2]

Structures
1GDD Conformation 1 [ PartsList ]

Description
Twenty-five residues from Asp9 to Glu33 along with eleven COOH-terminal residues fold into a compact microdomain at the NH2-terminal edge of the Ras domain beta sheet in one complex ( G(i alpha 1)-GDP (PDB id 1GDD) ) as compared with the another (the -GTPgS complex), although the overall canonical Ras-like alpha-beta fold is preserved in both conformations.

Particular values describing motion
Maximum CA displacement (A) = 2.1 (Greater than 2 angstroms.)
Experimental Methods = x (Traditional x-ray)
Creation Date = 19971130
Modification Date = 19971212

References
M B Mixon, E Lee, D E Coleman, A M Berghuis, A G Gilman, S R Sprang (1995). Tertiary and Quarternary Structural Changes in G(i alpha 1) Induced by GTP Hydrolysis. Sci. 270:954-960. [Medline info for 95050585]
H R Bourne (1995). Trimeric G Proteins: Surprise Witness Tells a Tale. Sci. 270:933-934. [Medline info for 95050585]

GO terms associated with structures
Molecular functionsignal transducer activity, GTP binding
Biological processG-protein coupled receptor protein signaling pathway, signal transduction

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Gialpha (GppNHP -> G 1cip [ A ] 1gp2 [ A ] 353

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
13077-15113 Gi-alpha 1cip [ A ] 1git [ A ] 353
30693-11614 Gi-alpha (GDP-Pi-Mg 1bof [ A ] 1git [ A ] 353
52160-29276 Gi-alpha (transition 1gfi [ A ] 1bof [ A ] 353
318221-20913 GiAlpha upload [ A ] upload [ A ] 325
98921-21548 Gialpha (GDP -> GDP- 1gdd [ A ] 1gp2 [ A ] 353
33492-14072 Gialpha (GdP-Pi -> G 1git [ A ] 1gdd [ A ] 353
25082-11656 Gialpha (GTP -> tran 1cip [ A ] 1gfi [ A ] 353


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