Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

Chun Tang, Charles D. Schwieters and G. Marius Clore ()
Additional contact information
Chun Tang: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA
Charles D. Schwieters: Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892-5624, USA
G. Marius Clore: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA

Nature, 2007, vol. 449, issue 7165, 1078-1082

Abstract: It is well known that large-scale rearrangements of domains of a protein can play an important role in ligand binding and recognition, catalysis, and regulation. Though X-ray crystal structures can provide a static picture of the apo (usually open) and holo (usually closed) states of a protein, it is not usually clear whether the apo state exists as a single species where the closed state is energetically inaccessible and interdomain rearrangement is induced by ligand or substrate binding or whether the predominantly open form already co-exists in rapid equilibrium with a minor closed species. In this paper, the authors obtained paramagnetic relaxation enhancement data that indicate that there is a rapidly exchanging mixture of a predominantly open form of the maltose-binding protein and a minor (partially-closed) form of the protein. Ensemble simulated annealing refinement was used to determine an ensemble average structure of the minor apo species and demonstrate that it is distinct from the sugar-bound state.

Date: 2007
References: Add references at CitEc
Citations: View citations in EconPapers (8)

Downloads: (external link)
https://www.nature.com/articles/nature06232 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:449:y:2007:i:7165:d:10.1038_nature06232

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature06232

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().