1e34: Difference between revisions
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==PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA-TOLUENESULPHONYL-3-ETHYL-4-(CARBOXYLIC ACID) PYRROLIDIN-2-ONE SOAKED IN PH 9 BUFFER FOR ONE MINUTE== | |||
==PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA- TOLUENESULPHONYL-3-ETHYL-4-(CARBOXYLIC ACID) PYRROLIDIN-2-ONE SOAKED IN PH 9 BUFFER FOR ONE MINUTE== | |||
<StructureSection load='1e34' size='340' side='right' caption='[[1e34]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1e34' size='340' side='right' caption='[[1e34]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3est|3est]], [[1qgf|1qgf]], [[1e35|1e35]], [[1e36|1e36]], [[1e37|1e37]], [[1e38|1e38]], [[1est|1est]], [[2est|2est]], [[4est|4est]], [[5est|5est]], [[6est|6est]], [[7est|7est]], [[8est|8est]], [[9est|9est]], [[1inc|1inc]], [[1jim|1jim]], [[1ela|1ela]], [[1elb|1elb]], [[1elc|1elc]], [[1eld|1eld]], [[1ele|1ele]], [[1elf|1elf]], [[1elg|1elg]], [[1esa|1esa]], [[1esb|1esb]], [[1eai|1eai]], [[1eas|1eas]], [[1eat|1eat]], [[1eau|1eau]], [[1bma|1bma]], [[1lvy|1lvy]], [[1nes|1nes]], [[1b0e|1b0e]], [[1btu|1btu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3est|3est]], [[1qgf|1qgf]], [[1e35|1e35]], [[1e36|1e36]], [[1e37|1e37]], [[1e38|1e38]], [[1est|1est]], [[2est|2est]], [[4est|4est]], [[5est|5est]], [[6est|6est]], [[7est|7est]], [[8est|8est]], [[9est|9est]], [[1inc|1inc]], [[1jim|1jim]], [[1ela|1ela]], [[1elb|1elb]], [[1elc|1elc]], [[1eld|1eld]], [[1ele|1ele]], [[1elf|1elf]], [[1elg|1elg]], [[1esa|1esa]], [[1esb|1esb]], [[1eai|1eai]], [[1eas|1eas]], [[1eat|1eat]], [[1eau|1eau]], [[1bma|1bma]], [[1lvy|1lvy]], [[1nes|1nes]], [[1b0e|1b0e]], [[1btu|1btu]]</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='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=1e34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e34 OCA], [http://pdbe.org/1e34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e34 RCSB], [http://www.ebi.ac.uk/pdbsum/1e34 PDBsum]</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=1e34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e34 OCA], [http://pdbe.org/1e34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e34 RCSB], [http://www.ebi.ac.uk/pdbsum/1e34 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e34 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/1e34_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/1e34_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1e34" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1e34" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:01, 13 December 2017
PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA- TOLUENESULPHONYL-3-ETHYL-4-(CARBOXYLIC ACID) PYRROLIDIN-2-ONE SOAKED IN PH 9 BUFFER FOR ONE MINUTEPORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA- TOLUENESULPHONYL-3-ETHYL-4-(CARBOXYLIC ACID) PYRROLIDIN-2-ONE SOAKED IN PH 9 BUFFER FOR ONE MINUTE
Structural highlights
Function[CELA1_PIG] Acts upon elastin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedbeta-Lactams inhibit a range of enzymes via acylation of nucleophilic serine residues. Certain gamma-lactam analogues of monocyclic beta-lactams have also been shown to be reversible inhibitors of porcine pancreatic elastase (PPE), forming acyl-enzyme complexes that are stable with respect to hydrolysis. Crystallographic analysis at pH 5 of an acyl-enzyme complex formed with PPE and one of these inhibitors revealed the ester carbonyl located in the oxyanion hole in a similar conformation to that observed in the structure of a complex formed between a heptapeptide (beta-casomorphin-7) and PPE. Only weak electron density was observed for the His-57 side chain in its 'native' conformation. Instead, the His-57 side chain predominantly adopted a conformation rotated approx. 90 degrees from its normal position. PPE-gamma-lactam crystals were subjected to 'pH-jumps' by placing the crystals in a buffer of increased pH prior to freezing for data collection. The results indicate that the conformation of the gamma-lactam-derived acyl-enzyme species in the PPE active site is dependent on pH, a result having implications for the analysis of other serine protease-inhibitor structures at non-catalytic pH values. The results help to define the stereoelectronic relationship between the ester of the acyl-enzyme complex, the side chain of His-57 and the incoming nucleophile during the reversible (de)acylation steps, implying it is closely analogous to the hydrolytic deacylation step during catalytic peptide hydrolysis. 'pH-jump' crystallographic analyses of gamma-lactam-porcine pancreatic elastase complexes.,Wright PA, Wilmouth RC, Clifton IJ, Schofield CJ Biochem J. 2000 Oct 15;351 Pt 2:335-40. PMID:11023818[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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