1omp
From Proteopedia
CRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND CHEMOTAXIS
Template:ABSTRACT PUBMED 1420181
About this Structure
1omp is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry. 1992 Nov 10;31(44):10657-63. PMID:1420181
- Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature. 2007 Nov 22;450(7169):515-21. PMID:18033289 doi:10.1038/nature06264
