Motion in Phosphofructokinase (PFK) (not allosteric transition) [pfknotal]

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Classification Known Domain Motion, Shear Mechanism [D-s-2]

Structures 1PFK Conformation 1 [ PartsList ]

Description Each PFK subunit consists of two domains. Comparison of the 2 R-state subunits in the asymmetric unit, shows that one is more closed than other. This small domain closure shifts CA atoms up to 3.5 A and involves and overall rotation of 5.5 degrees and an overall translation of 0.45 A. Despite the identification of a clear rotation axis, the motion is best described as proceeding through a shear mechanism. Three helices (2, 4, and 5) on the outer layer of the protein shift slightly and a loop changes conformation. This motion changes the geometry of the active site slightly but is NOT thought to be related to the allosteric transition.

Particular values describing motion Creation Date = 19970822 Modification Date = 19970822 Experimental Methods = x (Traditional x-ray)

References Y Shirakihara and P R Evans (1988). Crystal Structure of the Complex of Phosphofructokinase from Escherichia coli With its Reaction Products. J. Mol. Biol. 204: 973-994. [Medline info for 89125622]

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