8gch

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{{Seed}}
 
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[[Image:8gch.png|left|200px]]
 
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==GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN AUTOLYSIS PRODUCTS==
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The line below this paragraph, containing "STRUCTURE_8gch", creates the "Structure Box" on the page.
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<StructureSection load='8gch' size='340' side='right'caption='[[8gch]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_8gch| PDB=8gch | SCENE= }}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gc/8gch_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN AUTOLYSIS PRODUCTS===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8gch" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_2036388}}, adds the Publication Abstract to the page
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*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 2036388 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_2036388}}
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__TOC__
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</StructureSection>
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Chymotrypsin]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Harel M]]
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[[Category: Harel, M.]]
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[[Category: Silman I]]
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[[Category: Silman, I.]]
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[[Category: Sussman JL]]
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[[Category: Sussman, J L.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 12:07:22 2008''
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Current revision

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

PDB ID 8gch

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