Motion in Phosphoglycerate Kinase [pgk]

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

Structures 13PK Closed ternary [ PartsList ] 1PHP Open binary [ PartsList ] 2PGK Open apo

Description A 32 degree hinge motion with a positional displacement of up to 27 angstrom between open and closed crystal structures is observed. This, and the residue numbering below, refers to the closed trypanosomal structure (13PK). The actual hinge bending motion shown in the movie was modelled by biased molecular dynamics without knowledge of the closed conformation. Key hinge motions were observed but the extent of closing was slightly exaggerated.

Particular values describing motion Creation Date = 1999-03-31 Domain 1 (residue selection) = 5-194, 411 Domain 2 (residue selection) = 211-394 Location of a Hinge (residue selection) = 195-210, 3 Maximum CA displacement (A) = 27 Maximum Rotation (degrees) = 32 Number of hinges = 2 Modification Date = 1999-04-01 03:49:26.000

References A general method of domain closure is applied to phosphoglycerate kinase and the result compared with the crystal structure of a closed conformation of the enzyme. N.R. Chandra, H. Muirhead, J.J. Holbrook, B.E. Bernstein, W.G.J. Hol & R.B. Sessions. Proteins 30 (1998) 372-380. [Medline info for 89125622] Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. B.E. Bernstein, P.A. Michels & W.G.J. Hol. Nature 385 (1997) 275-278. [Medline info for 89125622]

Data and Graphics Hinge bending movie A GIF animation of the molecular dynamics Richard B. Sessions Home Page Please contact r.sessions@bris.ac.uk regarding this entry

GO terms associated with structures Molecular function phosphoglycerate kinase activity Biological process glycolysis

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