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TitleInsights into the Conformational Equilibria of Maltose-binding Protein by Analysis of High Affinity Mutants.
Journal, issue, pagesJ. Biol. Chem., Vol. 278, Page 34555-34567, Year 2003
Publish dateOct 29, 2002 (structure data deposition date)
AuthorsTelmer, P.G. / Shilton, B.H.
External linksJ. Biol. Chem. / PubMed:12794084
MethodsX-ray diffraction
Resolution2.1 - 2.6 Å
Structure data

PDB-1n3w:
Engineered High-Affinity Maltose-Binding Protein
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-1n3x:
Ligand-free High-Affinity Maltose-Binding Protein
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1nl5:
Engineered High-affinity Maltose-Binding Protein
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1peb:
LIGAND-FREE HIGH-AFFINITY MALTOSE-BINDING PROTEIN
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsSUGAR BINDING PROTEIN / MBP / Maltose-Binding Protein / High-Affinity Mutant / Engineered / MBPdel-liganded / MBPdel / Engineered mutant / MBPdel-unliganded / High-Affinity / conformational engineering / Maltodextrin-Binding Protein

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