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1aks

From Proteopedia

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{{STRUCTURE_1aks| PDB=1aks | SCENE= }}
{{STRUCTURE_1aks| PDB=1aks | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN'''
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===CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15299934}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15299934 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15299934}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:23:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:03:29 2008''

Revision as of 14:03, 30 June 2008

Image:1aks.png

Template:STRUCTURE 1aks

CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN

Template:ABSTRACT PUBMED 15299934

About this Structure

1AKS is a Protein complex structure of sequences from Sus scrofa. 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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