1aks: Difference between revisions

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New page: left|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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[[Image:1aks.jpg|left|200px]]<br /><applet load="1aks" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1aks.jpg|left|200px]]<br /><applet load="1aks" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1aks, resolution 1.8&Aring;" />
caption="1aks, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN'''<br />
'''CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN'''<br />


==Overview==
==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.
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==
==About this Structure==
1AKS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AKS OCA].  
1AKS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AKS OCA].  


==Reference==
==Reference==
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[[Category: Krishnaswamy, S.]]
[[Category: Krishnaswamy, S.]]
[[Category: Pattabhi, V.]]
[[Category: Pattabhi, V.]]
[[Category: Sundaram, P.V.]]
[[Category: Sundaram, P V.]]
[[Category: CA]]
[[Category: CA]]
[[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 Thu Feb 21 11:45:38 2008''

Revision as of 12:45, 21 February 2008

File:1aks.jpg


1aks, resolution 1.8Å

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

OverviewOverview

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 StructureAbout this Structure

1AKS is a Protein complex structure of sequences from Sus scrofa with as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

ReferenceReference

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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