Abstract:
:Ligand-induced conformational change in transferrins has been studied by site-directed mutagenesis of human serum half molecule (N-lobe), X-ray absorption fine structure (XAFS) spectroscopy and X-ray solution scattering. Use of recent advances in data analysis has been made for extracting model-independent molecular shapes from X-ray solution scattering data for the intact, the half molecule and its mutants. Clear evidence is provided that the transferrin molecule (intact as well as N-lobe), in its apo and holo forms, exists for the majority of the time in well-defined specific conformations representing the "fully opened" and "closed" states of the molecule, respectively. Evidence is also provided for the existence of an additional conformation, referred to here as the "intermediate" conformation for simplicity, which is trapped in the case of some of the mutants in the iron-bound form. We suggest that domain closure in the transferrin molecule is a two-step process, with the intermediate conformation representing the first stage of domain closure (approximately 20 degrees hinge-twist of domain II). Our data are not inconsistent with the ligand-free molecule sampling the closed states occasionally (< or = 10%) but are not in support of a continuous conformational search between the fully opened and closed states in the absence of iron.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Grossmann JG,Crawley JB,Strange RW,Patel KJ,Murphy LM,Neu M,Evans RW,Hasnain SSdoi
10.1006/jmbi.1998.1787subject
Has Abstractpub_date
1998-06-05 00:00:00pages
461-72issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(98)91787-9journal_volume
279pub_type
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