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[[Image:8gch.gif|left|200px]]


{{Structure
==GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN AUTOLYSIS PRODUCTS==
|PDB= 8gch |SIZE=350|CAPTION= <scene name='initialview01'>8gch</scene>, resolution 1.6&Aring;
<StructureSection load='8gch' size='340' side='right'caption='[[8gch]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[8gch]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GCH FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gch OCA], [https://pdbe.org/8gch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gch RCSB], [https://www.ebi.ac.uk/pdbsum/8gch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gch ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gc/8gch_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=8gch ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''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.,Harel M, Su CT, Frolow F, Silman I, Sussman JL Biochemistry. 1991 May 28;30(21):5217-25. PMID:2036388<ref>PMID:2036388</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8gch" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
 
== References ==
==About this Structure==
<references/>
8GCH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GCH OCA].
__TOC__
 
</StructureSection>
==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:[http://www.ncbi.nlm.nih.gov/pubmed/2036388 2036388]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Chymotrypsin]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Harel M]]
[[Category: Harel, M.]]
[[Category: Silman I]]
[[Category: Silman, I.]]
[[Category: Sussman JL]]
[[Category: Sussman, J L.]]
[[Category: hydrolase (serine proteinase)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:45:09 2008''

Latest revision as of 08:55, 5 June 2024

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

Structural highlights

8gch is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CTRA_BOVIN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Harel M, Su CT, Frolow F, Silman I, Sussman JL. Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products. Biochemistry. 1991 May 28;30(21):5217-25. PMID:2036388

8gch, resolution 1.60Å

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