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Structure paper

TitleA Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies.
Journal, issue, pagesJ. Biol. Chem., Vol. 265, Page 16592-16603, Year 1990
Publish dateNov 15, 1991 (structure data deposition date)
AuthorsVermersch, P.S. / Tesmer, J.J. / Lemon, D.D. / Quiocho, F.A.
External linksPubMed:2204627
MethodsX-ray diffraction
Resolution1.75 - 1.97 Å
Structure data

PDB-1apb:
A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES
Method: X-RAY DIFFRACTION / Resolution: 1.76 Å

PDB-1bap:
A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-9abp:
A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

Chemicals

ChemComp-FCA:
alpha-D-fucopyranose

ChemComp-FCB:
beta-D-fucopyranose

ChemComp-HOH:
WATER

ChemComp-ARA:
alpha-L-arabinopyranose

ChemComp-ARB:
beta-L-arabinopyranose

ChemComp-GLA:
alpha-D-galactopyranose

ChemComp-GAL:
beta-D-galactopyranose

Source
  • escherichia coli (E. coli)
KeywordsBINDING PROTEINS

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