8gch

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[[Image:8gch.gif|left|200px]]
[[Image:8gch.gif|left|200px]]
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{{Structure
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|PDB= 8gch |SIZE=350|CAPTION= <scene name='initialview01'>8gch</scene>, resolution 1.6&Aring;
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The line below this paragraph, containing "STRUCTURE_8gch", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span>
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{{STRUCTURE_8gch| PDB=8gch | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=8gch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gch OCA], [http://www.ebi.ac.uk/pdbsum/8gch PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=8gch RCSB]</span>
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'''GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN AUTOLYSIS PRODUCTS'''
'''GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN AUTOLYSIS PRODUCTS'''
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[[Category: Silman, I.]]
[[Category: Silman, I.]]
[[Category: Sussman, J L.]]
[[Category: Sussman, J L.]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:49:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:45:09 2008''
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Revision as of 19:49, 4 May 2008

Image:8gch.gif

Template:STRUCTURE 8gch

GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN AUTOLYSIS PRODUCTS


Overview

The determination of three separate gamma-chymotrypsin structures at different temperatures and resolutions confirmed the presence of electron density in the active site, which could be interpreted as an oligopeptide as had previously been suggested by Dixon and Matthews [(1989) Biochemistry 28, 7033-7038]. HPLC analyses of the enzyme before and after crystallization demonstrated the presence of a wide variety of oligopeptides in the redissolved crystal, most with COOH-terminal aromatic residues, as expected of the products of chymotrypsin cleavage, which appeared to arise from extensive autolysis of the enzyme under the crystallization conditions. The refined structures agree well with the conformation of both gamma-chymotrypsin and alpha-chymotrypsin. The electron density in the active site is thus interpreted as arising from a repertoire of autolysed oligopeptides produced concomitantly with crystallization. The COOH-terminal carbons of the polypeptide(s) display short contact distances (1.97, 2.47, and 2.13 A, respectively) to Ser195 O gamma in all three refined structures, but the electron density is not continuous between these two atoms in any of them. This suggests that some sequences are covalently bound as enzyme intermediates while others are noncovalently bound as enzyme-product complexes.

About this Structure

8GCH is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products., Harel M, Su CT, Frolow F, Silman I, Sussman JL, Biochemistry. 1991 May 28;30(21):5217-25. PMID:2036388 Page seeded by OCA on Sun May 4 22:49:17 2008

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