1b2f
PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.98 COORDINATES)
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OverviewOverview
Structures of porcine insulin crystals soaked in 1 M sodium sulfate at pH, 5.00, 5.53, 5.80, 6.00, 6.16, 6.26, 6.35, 6.50, 6.98 and 9.00 have been, determined at between 1.7 and 1.9 A resolution. GluB13 exhibits a single, conformation at pH </= 5.80, two conformations between pH 6.00 and 6.98, and a single conformation at pH 9.00. Between pH 6.00 and 6.98, the, conformation of GluB13 switches from one rotamer to another rotamer., Between pH 6.16 and 6.26, PheB1 undergoes a significant conformational, change. By pH 9.00 many residues have undergone relatively large shifts, and HisB10 exhibits a double conformation. As a result of the pH increase, the occupancy of the sulfate ion decreases from a maximum of 1.00 at pH, 5.00 to a minimum of 0.46 at pH 6.50. Comparison of the structures, the, observed and calculated structure factors and map correlation coefficients, indicate that the porcine insulin structure changes gradually as a, function of pH.
About this StructureAbout this Structure
1B2F is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding., Diao J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):670-6. Epub 2003, Mar 25. PMID:12657786
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