4gch

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(New page: 200px<br /><applet load="4gch" size="450" color="white" frame="true" align="right" spinBox="true" caption="4gch, resolution 1.9&Aring;" /> '''STRUCTURE AND ACTIVIT...)
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[[Image:4gch.jpg|left|200px]]<br /><applet load="4gch" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4gch, resolution 1.9&Aring;" />
 
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'''STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN'''<br />
 
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==Overview==
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==STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN==
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The serine protease gamma-chymotrypsin was covalently inhibited with two, different photoreversible cinnamate compounds, and the structures of the, resulting complexes were determined to 1.9-A resolution. The inhibitors, show different kinetics of binding, inhibition, and nonphotochemical, deacylation relative to each other in solution activity assays. The, crystal structures of the enzyme-cinnamate complexes show that both, compounds acylate serine 195 and that the two molecules are bound in, similar nonproductive conformations which have drastic effects on their, ability to turn over. Substitution of a diethylamino group on the para, position of the cinnamate ring causes a 1000-fold increase in the thermal, stability of the inhibitor toward hydrolysis and deacylation.
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<StructureSection load='4gch' size='340' side='right'caption='[[4gch]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4gch]] is a 3 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=4GCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GCH FirstGlance]. <br>
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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]] 1.9&#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=DMC:3-(4-DIETHYLAMINO-2-HYDROXY-PHENYL)-2-METHYL-PROPIONIC+ACID'>DMC</scene></td></tr>
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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=4gch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gch OCA], [https://pdbe.org/4gch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gch RCSB], [https://www.ebi.ac.uk/pdbsum/4gch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gch 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/4gch_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=4gch 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 serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation.
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==About this Structure==
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Structure and activity of two photoreversible cinnamates bound to chymotrypsin.,Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA Biochemistry. 1990 May 22;29(20):4871-9. PMID:2364065<ref>PMID:2364065</ref>
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4GCH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with DMC as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4GCH OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure and activity of two photoreversible cinnamates bound to chymotrypsin., Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 May 22;29(20):4871-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2364065 2364065]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 4gch" style="background-color:#fffaf0;"></div>
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[[Category: Chymotrypsin]]
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[[Category: Protein complex]]
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[[Category: Petsko, G.A.]]
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[[Category: Ringe, D.]]
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[[Category: Stoddard, B.L.]]
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[[Category: DMC]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:37:01 2007''
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==See Also==
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*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Petsko GA]]
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[[Category: Ringe D]]
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[[Category: Stoddard BL]]

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STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN

PDB ID 4gch

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