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 functionlysozyme activity
Biological processpeptidoglycan catabolism, cell wall catabolism

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
1l96 [ ] 1l97 [ ] 164

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
341910-19675 T4 209l [ A ] 7lzm [ A ] 164
341965-19697 T4_2 209l [ A ] 7lzm [ A ] 164

Automatic morphs
Morph Morph name Structure #1 Structure #2 Residues
va1l18A-172lA Lysozyme (E.C. 3.2.1.17) (Muta 1l18 [ A ] 172l [ A ] 164
va1l17A-172lA Lysozyme (E.C. 3.2.1.17) (Muta 1l17 [ A ] 172l [ A ] 164
va2lzmA-172lA Lysozyme (E.C. 3.2.1.17) - Cha 2lzm [ A ] 172l [ A ] 164
va3lzmA-172lA Lysozyme (E.C. 3.2.1.17) - Cha 3lzm [ A ] 172l [ A ] 164
va2lzmA-1l97B Lysozyme (E.C. 3.2.1.17) - Cha 2lzm [ A ] 1l97 [ B ] 164
va2lzmA-1l97A Lysozyme (E.C. 3.2.1.17) - Cha 2lzm [ A ] 1l97 [ A ] 164
va2lzmA-149lA Lysozyme (E.C. 3.2.1.17) - Cha 2lzm [ A ] 149l [ A ] 164
va3lzmA-149lA Lysozyme (E.C. 3.2.1.17) - Cha 3lzm [ A ] 149l [ A ] 164
va1l97A-3lzmA Lysozyme (E.C. 3.2.1.17) Mutan 1l97 [ A ] 3lzm [ A ] 164
va172lA-1lydA Lysozyme (E.C. 3.2.1.17) Mutan 172l [ A ] 1lyd [ A ] 164
va1l97B-1l18A Lysozyme (E.C. 3.2.1.17) Mutan 1l97 [ B ] 1l18 [ A ] 164
va1l97A-1l17A Lysozyme (E.C. 3.2.1.17) Mutan 1l97 [ A ] 1l17 [ A ] 164
va1l97A-1l18A Lysozyme (E.C. 3.2.1.17) Mutan 1l97 [ A ] 1l18 [ A ] 164
va1l97B-1l17A Lysozyme (E.C. 3.2.1.17) Mutan 1l97 [ B ] 1l17 [ A ] 164
va1l97B-3lzmA Lysozyme (E.C. 3.2.1.17) Mutan 1l97 [ B ] 3lzm [ A ] 164
va149lA-1l18A Lysozyme (E.C. 3.2.1.17) Mutan 149l [ A ] 1l18 [ A ] 164
va149lA-172lA Lysozyme (E.C. 3.2.1.17) Mutan 149l [ A ] 172l [ A ] 164
va149lA-1l17A Lysozyme (E.C. 3.2.1.17) Mutan 149l [ A ] 1l17 [ A ] 164
va1lydA-1l97A T4-Lysozyme - Chain _ 1lyd [ A ] 1l97 [ A ] 164
va1lydA-1l97B T4-Lysozyme - Chain _ 1lyd [ A ] 1l97 [ B ] 164
va1lydA-149lA T4-Lysozyme - Chain _ 1lyd [ A ] 149l [ A ] 164

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