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New page: left|200px<br /><applet load="1esa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esa, resolution 1.65Å" /> '''DIRECT STRUCTURE OBS...
 
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[[Image:1esa.gif|left|200px]]<br /><applet load="1esa" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1esa, resolution 1.65&Aring;" />
'''DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE'''<br />


==Overview==
==DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE==
The method of X-ray crystallographic cryoenzymology has been used to, determine the crystal structure of a kinetically significant species on, the reaction pathway of a crystalline enzyme. The structure of a specific, acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of the, N-carbobenzoxy-L-alanine p-nitrophenyl ester has been determined and, refined against X-ray diffraction data at 2.3-A resolution. The difference, Fourier electron density map clearly shows electron density for the, trapped acyl-enzyme. The acyl-enzyme was formed at -26 degrees C and was, stabilized at -55 degrees C during data collection, taking advantage of, the glass transition in protein dynamics that occurs at around -50 degrees, C.
<StructureSection load='1esa' size='340' side='right'caption='[[1esa]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1esa]] 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=1ESA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esa OCA], [https://pdbe.org/1esa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esa RCSB], [https://www.ebi.ac.uk/pdbsum/1esa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esa 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/es/1esa_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=1esa ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The method of X-ray crystallographic cryoenzymology has been used to determine the crystal structure of a kinetically significant species on the reaction pathway of a crystalline enzyme. The structure of a specific acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of the N-carbobenzoxy-L-alanine p-nitrophenyl ester has been determined and refined against X-ray diffraction data at 2.3-A resolution. The difference Fourier electron density map clearly shows electron density for the trapped acyl-enzyme. The acyl-enzyme was formed at -26 degrees C and was stabilized at -55 degrees C during data collection, taking advantage of the glass transition in protein dynamics that occurs at around -50 degrees C.


==About this Structure==
Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase.,Ding X, Rasmussen BF, Petsko GA, Ringe D Biochemistry. 1994 Aug 9;33(31):9285-93. PMID:8049229<ref>PMID:8049229</ref>
1ESA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase., Ding X, Rasmussen BF, Petsko GA, Ringe D, Biochemistry. 1994 Aug 9;33(31):9285-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8049229 8049229]
</div>
[[Category: Pancreatic elastase]]
<div class="pdbe-citations 1esa" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
 
==See Also==
*[[Elastase 3D structures|Elastase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Ding, X.]]
[[Category: Ding X]]
[[Category: Petsko, G.A.]]
[[Category: Petsko GA]]
[[Category: Rasmussen, B.]]
[[Category: Rasmussen B]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: CA]]
[[Category: SO4]]
[[Category: hydrolase(serine proteinase)]]
 
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Retrieved from "https://proteopedia.org/1esa"