View source for 1elg

==NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH==
<StructureSection load='1elg' size='340' side='right' caption='[[1elg]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1elg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ELG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BAA:(TERT-BUTYLOXYCARBONYL)-ALANYL-ALANYL-AMINE'>BAA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elg OCA], [http://pdbe.org/1elg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1elg RCSB], [http://www.ebi.ac.uk/pdbsum/1elg PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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/el/1elg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
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== Publication Abstract from PubMed ==
The mechanism of inactivation of porcine pancreatic elastase (PPE) by N-peptidyl-O-aroylhydroxylamine was studied by X-ray crystallography. The inactivator forms a stable complex with the enzyme by means of a covalent attachment to the active site Ser 203(195) O gamma. The nature of the complex is, however, different depending on the pH at which the inactivation reaction occurs. At pH 5, the complex formed is a hydroxylamine derivative of Ser 203(195) in which the O gamma of serine is the oxygen of the hydroxylamine derivative. At pH 7.5, the complex formed is a carbamate derivative at Ser 203(195) O gamma. In both types of complexes, the inactivator binds in the S' subsites of the enzyme instead of forming the usual antiparallel beta-sheet with the S subsites. The implication for the mechanism of inactivation at different pHs is discussed.

Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH.,Ding X, Rasmussen BF, Demuth HU, Ringe D, Steinmetz AC Biochemistry. 1995 Jun 13;34(23):7749-56. PMID:7779821<ref>PMID:7779821</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1elg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elastase|Elastase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Pancreatic elastase]]
[[Category: Pig]]
[[Category: Demuth, H U]]
[[Category: Ding, X]]
[[Category: Rasmussen, B]]
[[Category: Ringe, D]]
[[Category: Steinmetz, A C.U]]