1e37: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e37]] 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=1E37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E37 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e37]] 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=1E37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E37 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPY:(2S,3S)-3-FORMYL-2-({[(4-NITROPHENYL)SULFONYL]AMINO}METHYL)PENTANOIC+ACID'>TPY</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPY:(2S,3S)-3-FORMYL-2-({[(4-NITROPHENYL)SULFONYL]AMINO}METHYL)PENTANOIC+ACID'>TPY</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3est|3est]], [[1qgf|1qgf]], [[1e34|1e34]], [[1e35|1e35]], [[1e36|1e36]], [[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]], [[1e34|1e34]], [[1e35|1e35]], [[1e36|1e36]], [[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><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e37 RCSB], [http://www.ebi.ac.uk/pdbsum/1e37 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=1e37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e37 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e37 RCSB], [http://www.ebi.ac.uk/pdbsum/1e37 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Pancreatic elastase]] | [[Category: Pancreatic elastase]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Clifton, I J | [[Category: Clifton, I J]] | ||
[[Category: Schofield, C J | [[Category: Schofield, C J]] | ||
[[Category: Wilmouth, R C | [[Category: Wilmouth, R C]] | ||
[[Category: Wright, P A | [[Category: Wright, P A]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
[[Category: Serine proteinase]] | [[Category: Serine proteinase]] | ||
Revision as of 21:43, 22 December 2014
PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA-NITROBENZENESULPHONYL -3-ETHYL-4-(CARBOXYLIC ACID)PYRROLIDIN-2-ONE SOAKED IN PH 9 BUFFER FOR 1 MINUTEPORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA-NITROBENZENESULPHONYL -3-ETHYL-4-(CARBOXYLIC ACID)PYRROLIDIN-2-ONE SOAKED IN PH 9 BUFFER FOR 1 MINUTE
Structural highlights
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. See AlsoReferences |
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