1elf
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | [[ | + | ==NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH== |
+ | <StructureSection load='1elf' size='340' side='right' caption='[[1elf]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1elf]] is a 1 chain structure 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=1ELF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ELF FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BAF:(TERT-BUTYLOXYCARBONYL)-ALANYL-AMINO+ETHYL-FORMAMIDE'>BAF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
+ | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1elf RCSB], [http://www.ebi.ac.uk/pdbsum/1elf PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == 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/1elf_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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
==See Also== | ==See Also== | ||
*[[Elastase|Elastase]] | *[[Elastase|Elastase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Pancreatic elastase]] | [[Category: Pancreatic elastase]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] |
Revision as of 11:12, 24 September 2014
NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH
|