1bzx: Difference between revisions
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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[[Image:1bzx.jpg|left|200px]]<br /><applet load="1bzx" size=" | [[Image:1bzx.jpg|left|200px]]<br /><applet load="1bzx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1bzx, resolution 2.1Å" /> | caption="1bzx, resolution 2.1Å" /> | ||
'''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 | 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:// | 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 | [[Category: Berglund, G I.]] | ||
[[Category: Helland, R.]] | [[Category: Helland, R.]] | ||
[[Category: Leiros, I.]] | [[Category: Leiros, I.]] | ||
[[Category: Smalas, A | [[Category: Smalas, A O.]] | ||
[[Category: Willassen, N | [[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:// | ''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
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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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