1hax

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[[Image:1hax.gif|left|200px]]
 
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{{Structure
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==Snapshots of serine protease catalysis: (A) acyl-enzyme intermediate between porcine pancreatic elastase and human beta-casomorphin-7 at pH 5==
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|PDB= 1hax |SIZE=350|CAPTION= <scene name='initialview01'>1hax</scene>, resolution 1.6&Aring;
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<StructureSection load='1hax' size='340' side='right'caption='[[1hax]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE= <scene name='pdbsite=CAT:Active+Site+Catalytic+Triad'>CAT</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1hax]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HAX FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.4.21.36 Transferred entry: 3.4.21.36], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.11 3.4.21.11]
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1hax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hax OCA], [https://pdbe.org/1hax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hax RCSB], [https://www.ebi.ac.uk/pdbsum/1hax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hax ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin.
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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/ha/1hax_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1hax 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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Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues. An oxyanion hole, consisting of the peptide amide of the active site serine and a neighbouring glycine, was identified, and hydrogen bonding in the oxyanion hole was suggested to stabilize the two proposed tetrahedral intermediates on the catalytic pathway. Here we show electron density changes consistent with the formation of a tetrahedral intermediate during the hydrolysis of an acyl-enzyme complex formed between a natural heptapeptide and elastase. No electron density for an enzyme-product complex was observed. The structures also suggest a mechanism for the synchronization of hydrolysis and peptide release triggered by the conversion of the sp2 hybridized carbonyl carbon to an sp3 carbon in the tetrahedral intermediate. This affects the location of the peptide in the active site cleft, triggering the collapse of a hydrogen bonding network between the peptide and the beta-sheet of the active site.
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'''SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (A) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 AT PH 5'''
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X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate.,Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:11473259<ref>PMID:11473259</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 1hax" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues. An oxyanion hole, consisting of the peptide amide of the active site serine and a neighbouring glycine, was identified, and hydrogen bonding in the oxyanion hole was suggested to stabilize the two proposed tetrahedral intermediates on the catalytic pathway. Here we show electron density changes consistent with the formation of a tetrahedral intermediate during the hydrolysis of an acyl-enzyme complex formed between a natural heptapeptide and elastase. No electron density for an enzyme-product complex was observed. The structures also suggest a mechanism for the synchronization of hydrolysis and peptide release triggered by the conversion of the sp2 hybridized carbonyl carbon to an sp3 carbon in the tetrahedral intermediate. This affects the location of the peptide in the active site cleft, triggering the collapse of a hydrogen bonding network between the peptide and the beta-sheet of the active site.
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*[[Elastase 3D structures|Elastase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1HAX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAX OCA].
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__TOC__
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</StructureSection>
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==Reference==
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X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11473259 11473259]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Transferred entry: 3 4.21 36]]
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[[Category: Clifton IJ]]
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[[Category: Clifton, I J.]]
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[[Category: Edman K]]
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[[Category: Edman, K.]]
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[[Category: Hajdu J]]
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[[Category: Hajdu, J.]]
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[[Category: Neutze R]]
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[[Category: Neutze, R.]]
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[[Category: Schneider TR]]
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[[Category: Schneider, T R.]]
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[[Category: Schofield CJ]]
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[[Category: Schofield, C J.]]
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[[Category: Wilmouth RC]]
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[[Category: Wilmouth, R C.]]
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[[Category: Wright PA]]
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[[Category: Wright, P A.]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: hydrolase (serine proteinase)]]
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[[Category: serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:38 2008''
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Current revision

Snapshots of serine protease catalysis: (A) acyl-enzyme intermediate between porcine pancreatic elastase and human beta-casomorphin-7 at pH 5

PDB ID 1hax

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