Motion in Maltodextrin Binding Protein (MBP) [mbp]

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

Structures
1OMF Conformation 1
2MBP Conformation 2

Description
3 interdomain linkages, 3 hinges, 35 degree rotation. The domain motion in the maltodextrin-binding protein is a 35 degree rotation about an axis through the hinge region, and there are large, localized torsion angle changes in the three peptides linking the domains. The positions of two of the hinges are structurally equivalent to the two hinges in lactoferrin.

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

References
A J Sharff, L E Rodseth, J C Spurlino and F A Quiocho (1992). Crystallographic Evidence of a Large Ligand-Induced Hinge-Twist Motion between the Two Domains of the Maltodextrin Binding Protein Involved in Active Transport and Chemotaxis. Biochemistry. 31: 10657-10663. [Medline info for 93041761]

Data and Graphics
Graphic-2 Graphic of overall motion courtesy of E S Huang.
Graphic-1 Hinge residues

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