Motion in Lactoferrin [lf]
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Classification Known Domain Motion, Hinge Mechanism [D-h-2]
Structures 1LFG Open Conformation [ PartsList ] 1LFH Closed Conformation [ PartsList ]
Description 2 interdomain linkages, 2 hinges (in a beta-sheet), 53 degree rotation. See-saw between two interfaces. Lactoferrin is an iron transport protein. Upon binding iron, the two domains in the N-terminal half of the molecule close, in a motion involving two hinges. Upon closure the domains rotate 54 degrees essentially as rigid bodies. The axis of rotation passes through the two beta-strands linking the domains. These strands contain hinges in the sense that three large torsion angle changes are responsible for the bulk of the motion while smaller torsion angle changes in neighboring residues are responsible for the remainder of the motion. The rotation axes of these three torsion angle changes are nearly parallel to the axis of the overall 54 degrees rotation, so the local motion in the hinges can be directly related to the overall motion. A crucial feature of the hinge residues is that they have very few packing constraints on their main-chain atoms. The domains make different packing contacts with each other in the open and closed forms. These contacts form two interdomain interfaces arranged on either side of the hinges. Pivoting about the hinges produces a see-saw motion between the two interfaces. That is, when the domains close down, residues in the interface on one side of the hinges become buried and close-packed and residues on the other side become exposed. The situation is reversed when the domains open up.
Particular values describing motion Domain 1 (residue selection) = 1-92 252-333 Domain 2 (residue selection) = 93-251 Location of a Hinge (residue selection) = 249-252 (second hinge) Location of a Hinge (residue selection) = 89-92 (first hinge) Experimental Methods = x (Traditional x-ray) Creation Date = 19970822 Modification Date = 19970822
References B F Anderson, H M Baker, G E Norris, S V Rumball and E N Baker (1990). Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. Nature. 344: 784-787. [Medline info for 91295198] M Gerstein, A M Lesk, E N Baker, B Anderson, G Norris and C Chothia (1993). Domain Closure in Lactoferrin: Two Hinges produce a See-saw Motion between Alternative Close-Packed Interfaces. J. Mol. Biol. 234: 357-372. [Medline info for 94047086]
Data and Graphics Graphic-1 The overall rotation, showing the tight packing of interfaces in the closed form. (Copyright Biochemistry, 1994) MOVIES A page giving pointers to movies of the motion.
GO terms associated with structures Molecular function ferric iron binding Cellular component extracellular region Biological process iron ion transport, iron ion homeostasis
Morphs[ show all images ]
Best representative Morph Morph name Structure #1 Structure #2 Residues Lactoferrin 1lfg [ A ] 1lfh [ A ] 691
User-submitted morphs Morph Morph name Structure #1 Structure #2 Residues 098438-24838 Camel Lactoferrin 1dtz [ A ] 1i6q [ A ] 689 100067-25743 Equus Lactoferrin 1b7u [ A ] 1b1x [ A ] 689 07730-19225 lactoferrin 1lfh [ A ] 1lfg [ A ] 691 lf Lactoferrin 1lfg [ A ] 1lfh [ A ] 691 636051-15611 Lactoferrin 1lfh [ A ] 1lfg [ A ] 691 636773-16645 Lactoferrin 1lfh [ A ] 1lfg [ A ] 691 75040-14359 Lactoferrin N-Lobe upload [ A ] upload [ A ] 333 75115-14394 Lactoferrin N-Lobe upload [ A ] upload [ A ] 333
Automatic morphs Morph Morph name Structure #1 Structure #2 Residues va1b1xA-1b7uA Lactoferrin 1b1x [ A ] 1b7u [ A ] 689 va1lfhA-1lfgA Lactoferrin (Apo Form) - Chain 1lfh [ A ] 1lfg [ A ] 691 va1lfhA-1b0lA Lactoferrin (Apo Form) - Chain 1lfh [ A ] 1b0l [ A ] 691 va1lcfA-1lfhA Lactoferrin (Copper and Oxalat 1lcf [ A ] 1lfh [ A ] 691 va1lfiA-1lfhA Lactoferrin (Copper Form) - Ch 1lfi [ A ] 1lfh [ A ] 691
Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu