Motion in Lysine/Arginine/Ornithine (LAO) binding protein [lao]

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

Structures
1LST Conformation 1 [ PartsList ]
2LAO Conformation2 [ PartsList ]

Description
2 interdomain linkages, 2 hinges, 52 degree rotation. In the LAO binding protein there is a 52 degree rotation of the two domains, which involves only a few large torsion angle changes in regions structurally equivalent to the lactoferrin hinges.

Particular values describing motion
Creation Date = 19970822
Experimental Methods = x (Traditional x-ray)
Modification Date = 1998-06-27 22:03:47.000

References
B-H Oh, J Pandit, C-H Kang, K Nikaido, S Gokcen, G F-L Ames and S-H Kim (1993). Three-dimensional structures of the Periplasmic Lysine/Arginine/Ornithine-binding Protein with and without a Ligand. J. Biol. Chem. 268: 11348-11355. [Medline info for 93266593]

GO terms associated with structures
Molecular functiontransporter activity
Cellular componentperiplasmic space (sensu Gram-negative Bacteria)
Biological processtransport

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
periplasmic lysine-, arginine-, ornithin 2lao [ ] 1laf [ ] 238

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
455165-24514 2LAO upload [ A ] upload [ A ] 237
455181-24542 2LAO upload [ A ] upload [ A ] 237
511105-11467 LAO upload [ A ] upload [ A ] 238
511454-12081 LAO upload [ A ] upload [ A ] 238
512137-14988 LAO upload [ A ] upload [ A ] 238
463147-30260 lysine arginine ornithine protein upload [ A ] upload [ A ] 238
770888-4288 lysine/arginine/ornithine-binding protei upload [ A ] upload [ A ] 239

Automatic morphs
Morph Morph name Structure #1 Structure #2 Residues
va2laoA-1lstA Lysine-, Arginine-, Ornithine- 2lao [ A ] 1lst [ A ] 239
va2laoA-1lafE Lysine-, Arginine-, Ornithine- 2lao [ A ] 1laf [ E ] 238
va2laoA-1lahE Lysine-, Arginine-, Ornithine- 2lao [ A ] 1lah [ E ] 238
va2laoA-1lagE Lysine-, Arginine-, Ornithine- 2lao [ A ] 1lag [ E ] 238

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