Motion in T4 lysozyme mutants: Ile3->Pro & Met6->Ile [lzm]

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

Structures 1L96 Conformation 1 [ PartsList ] 1L97 Conformation 2 [ PartsList ]

Description 2 hinges, at either end of interdomain helix, produce rotations up to 32 degrees. Depending on the crystal form, these 2 mutant lysozyme structures are either very similar to that of the wild-type or differ from it by a range of rigid-body domain rotations up to 32 degrees. There are two main hinge points for the domain motion. They occur at the ends of the long helix that spans the domains. The second hinge involves 8 small torsion angle changes (between 9 and 15 degrees) spread throughout the C-terminal part of the helix, bending it by 3.3 A. As the location of the mutation is next to the hinge, the domain motion appears to be a consequence of the loss of close-packing created by the mutation and is an example of hinged motion created by reducing the number of steric constraints.

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

References M M Dixon, H Nicholson, L Shewchuk, W A Baase and B W Matthews (1992). Structure of a Hinge-Bending Bacteriophage T4 Lysozyme Mutant, Ile3 to Pro. J. Mol. Biol. 227: 917-933. [Medline info for 92396238] H R Faber and B W Matthews (1990). A mutant T4 lysozyme displays five different crystal conformations. Nature. 348: 263-266. [Medline info for 91043097]

Data and Graphics Graphic-1 One of the hinges is a bending helix.

GO terms associated with structures Molecular function lysozyme activity Biological process cell wall catabolism, peptidoglycan catabolism

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