1aks
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(New page: 200px<br /><applet load="1aks" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aks, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 08:48, 20 November 2007
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CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN
Overview
The first crystal structure of an active autolysate form of porcine, alpha-trypsin (APT), a two-chain molecule obtained from the limited, autolysis of porcine beta-trypsin at position Lys145-Ser146, has been, determined. APT crystallizes in space group P2(1)2(1)2(1) 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 R(free) of 0.285 for 8.0-1.8 A data with r.m.s deviations from, ideal values of 0.01 A and 1.7 degrees for bond lengths and bond angles, respectively. Comparison with inactive autolysate porcine epsilon-trypsin, (EPT) and porcine beta-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.
About this Structure
1AKS is a Protein complex structure of sequences from Sus scrofa with CA as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin., Johnson A, Krishnaswamy S, Sundaram PV, Pattabhi V, Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):311-5. PMID:15299934
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