The First Structure at 1.8 Å Resolution of an Active Autolysate Form of Porcine α-Trysoin
Acta Crystallographica Section D
Volume 53, Issue 3, pages 311–315, May 1997
How to Cite
Johnson, A., Krishnaswamy, S., Sundaram, P. V. and Pattabhi, V. (1997), The First Structure at 1.8 Å Resolution of an Active Autolysate Form of Porcine α-Trysoin. Acta Crystallographica D, 53: 311–315. doi: 10.1107/S0907444997000358
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The first crystal structure of an active autolysate form of porcine α-trypsin (APT), a two-chain molecule obtained from the limited autolysis of porcine β-trypsin at position Lys145–Ser146, has been determined. APT crystallizes in space group P212121 with one protein molecule in the asymmetric unit. The structure was solved by molecular replacement followed by refinement using X-PLOR to an R factor of 0.200 and an Rfree of 0.285 for 8.0–1.8 Å data with r.m.s deviations from ideal values of 0.01 Å and 1.7° for bond lengths and bond angles, respectively. Comparison with inactive autolysate porcine ɛ-trypsin (EPT) and porcine β-trypsin in complex with bittergourd trypsin inhibitor (MCT) revealed a small but systematic directional chain shift around the active-site residues from APT to EPT to MCT.