1bzx: Difference between revisions

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New page: left|200px<br /><applet load="1bzx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bzx, resolution 2.1Å" /> '''THE CRYSTAL STRUCTURE...
 
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caption="1bzx, resolution 2.1&Aring;" />
caption="1bzx, resolution 2.1&Aring;" />
'''THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR'''<br />
'''THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR'''<br />


==Overview==
==Overview==
The complex formed between anionic salmon trypsin (ST) and bovine, pancreatic trypsin inhibitor (BPTI) has been crystallised, and the X-ray, structure has been solved using the molecular replacement method. The, crystals are hexagonal and belong to space group P6(1)22 with lattice, parameters of a = b = 83.12 A and c = 222.15 A. Data have been collected, to 2.1 A and the structure has been refined to a crystallographic R-factor, of 20.6%. Catalysis by salmon trypsin is distinguished by a Km value, 20-fold lower than that for mammalian trypsins, and a k(cat) twice as, high. The present ST-BPTI complex serves as a model for the, Michaelis-Menten complex, and has been compared with corresponding bovine, and rat trypsin (RT) complexes. The binding of BPTI to salmon trypsin is, characterised by stronger primary interactions in the active site, and a, somewhat looser secondary binding.
The complex formed between anionic salmon trypsin (ST) and bovine pancreatic trypsin inhibitor (BPTI) has been crystallised, and the X-ray structure has been solved using the molecular replacement method. The crystals are hexagonal and belong to space group P6(1)22 with lattice parameters of a = b = 83.12 A and c = 222.15 A. Data have been collected to 2.1 A and the structure has been refined to a crystallographic R-factor of 20.6%. Catalysis by salmon trypsin is distinguished by a Km value 20-fold lower than that for mammalian trypsins, and a k(cat) twice as high. The present ST-BPTI complex serves as a model for the Michaelis-Menten complex, and has been compared with corresponding bovine and rat trypsin (RT) complexes. The binding of BPTI to salmon trypsin is characterised by stronger primary interactions in the active site, and a somewhat looser secondary binding.


==About this Structure==
==About this Structure==
1BZX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Salmo_salar Salmo salar] 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=1BZX OCA].  
1BZX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Salmo_salar Salmo salar] 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=1BZX OCA].  


==Reference==
==Reference==
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[[Category: Salmo salar]]
[[Category: Salmo salar]]
[[Category: Trypsin]]
[[Category: Trypsin]]
[[Category: Berglund, G.I.]]
[[Category: Berglund, G I.]]
[[Category: Helland, R.]]
[[Category: Helland, R.]]
[[Category: Leiros, I.]]
[[Category: Leiros, I.]]
[[Category: Smalas, A.O.]]
[[Category: Smalas, A O.]]
[[Category: Willassen, N.P.]]
[[Category: Willassen, N P.]]
[[Category: CA]]
[[Category: CA]]
[[Category: cold adaptation]]
[[Category: cold adaptation]]
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[[Category: trypsin]]
[[Category: trypsin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:02:59 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:57 2008''

Revision as of 13:00, 21 February 2008

File:1bzx.jpg


1bzx, resolution 2.1Å

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THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR

OverviewOverview

The complex formed between anionic salmon trypsin (ST) and bovine pancreatic trypsin inhibitor (BPTI) has been crystallised, and the X-ray structure has been solved using the molecular replacement method. The crystals are hexagonal and belong to space group P6(1)22 with lattice parameters of a = b = 83.12 A and c = 222.15 A. Data have been collected to 2.1 A and the structure has been refined to a crystallographic R-factor of 20.6%. Catalysis by salmon trypsin is distinguished by a Km value 20-fold lower than that for mammalian trypsins, and a k(cat) twice as high. The present ST-BPTI complex serves as a model for the Michaelis-Menten complex, and has been compared with corresponding bovine and rat trypsin (RT) complexes. The binding of BPTI to salmon trypsin is characterised by stronger primary interactions in the active site, and a somewhat looser secondary binding.

About this StructureAbout this Structure

1BZX is a Protein complex structure of sequences from Bos taurus and Salmo salar with as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor., Helland R, Leiros I, Berglund GI, Willassen NP, Smalas AO, Eur J Biochem. 1998 Sep 1;256(2):317-24. PMID:9760170

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