Crystal Structures of the BtuF Periplasmic-binding Protein for Vitamin B12 Suggest a Functionally Important Reduction in Protein Mobility upon Ligand Binding
Open Access
- 1 March 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (10) , 8429-8434
- https://doi.org/10.1074/jbc.m212239200
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.Published by Elsevier ,2021
- ATP Binding to the Motor Domain from an ABC Transporter Drives Formation of a Nucleotide Sandwich DimerMolecular Cell, 2002
- The Crystal Structure of Zn(II)-Free Treponema pallidum TroA, a Periplasmic Metal-Binding Protein, Reveals a Closed ConformationJournal of Bacteriology, 2002
- Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transportProceedings of the National Academy of Sciences, 2001
- Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone.Nature Structural & Molecular Biology, 1999
- ATP hydrolysis cycles and mechanism inP-glycoprotein and CFTRSeminars in Cancer Biology, 1997
- STRUCTURE-BASED PERSPECTIVES ON B12-DEPENDENT ENZYMESAnnual Review of Biochemistry, 1997
- ABC Transporters: From Microorganisms to ManAnnual Review of Cell Biology, 1992
- Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxisBiochemistry, 1992
- Substrate specificity and affinity of a protein modulated by bound water moleculesNature, 1989