1hay: Difference between revisions

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-[[Image:1hay.png|left|200px]]
-<!--
+==Snapshots of serine protease catalysis: (B) acyl-enzyme intermediate between porcine pancreatic elastase and human beta-casomorphin-7 jumped to pH 10 for 10 seconds==
-The line below this paragraph, containing "STRUCTURE_1hay", creates the "Structure Box" on the page.
+<StructureSection load='1hay' size='340' side='right'caption='[[1hay]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1hay]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HAY FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
--->
+<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>
-{{STRUCTURE_1hay|  PDB=1hay  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hay OCA], [https://pdbe.org/1hay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hay RCSB], [https://www.ebi.ac.uk/pdbsum/1hay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hay ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin.
+== 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/ha/1hay_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1hay ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (B) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 JUMPED TO PH 10 FOR 10 SECONDS===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11473259}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1hay" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11473259 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_11473259}}
-==About this Structure==
-[[1hay]] is a 1 chain structure of [[Elastase]] with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAY OCA].
 ==See Also==
-*[[Elastase]]
+*[[Elastase 3D structures|Elastase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:11473259</ref><ref group="xtra">PMID:9187653</ref><ref group="xtra">PMID:3271103</ref><references group="xtra"/>
+__TOC__
-[[Category: Hydrolase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Sus scrofa]]
-[[Category: Clifton, I J.]]
+[[Category: Clifton IJ]]
-[[Category: Edman, K.]]
+[[Category: Edman K]]
-[[Category: Hajdu, J.]]
+[[Category: Hajdu J]]
-[[Category: Neutze, R.]]
+[[Category: Neutze R]]
-[[Category: Schneider, T R.]]
+[[Category: Schneider TR]]
-[[Category: Schofield, C J.]]
+[[Category: Schofield CJ]]
-[[Category: Wilmouth, R C.]]
+[[Category: Wilmouth RC]]
-[[Category: Wright, P A.]]
+[[Category: Wright PA]]
-[[Category: Hydrolase]]
-[[Category: Serine proteinase]]