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1gvk

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Revision as of 04:44, 21 September 2017

Porcine pancreatic elastase acyl enzyme at 0.95 A resolution

Structural highlights

1gvk is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1b0e, 1bma, 1btu, 1c1m, 1e34, 1e35, 1e36, 1e37, 1e38, 1e9h, 1eai, 1eas, 1eat, 1eau, 1ela, 1elb, 1elc, 1eld, 1ele, 1elf, 1elg, 1esa, 1esb, 1est, 1fle, 1fzz, 1h9l, 1hax, 1hay, 1haz, 1hb0, 1hv7, 1inc, 1jim, 1lvy, 1nes, 1qgf, 1qix, 1qnj, 1qr3, 2est, 3est, 4est, 5est, 6est, 7est, 8est, 9est
Activity:	Pancreatic elastase, with EC number 3.4.21.36
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Kinetic analyses led to the discovery that N-acetylated tripeptides with polar residues at P3 are inhibitors of porcine pancreatic elastase (PPE) that form unusually stable acyl-enzyme complexes. Peptides terminating in a C-terminal carboxylate were more potent than those terminating in a C-terminal amide, suggesting recognition by the oxy-anion hole is important in binding. X-ray diffraction data were recorded to 0.95-A resolution for an acyl-enzyme complex formed between PPE and N-acetyl-Asn-Pro-Ile-CO2H at approximately pH 5. The accuracy of the crystallographic coordinates allows structural issues concerning the mechanism of serine proteases to be addressed. Significantly, the ester bond of the acyl-enzyme showed a high level of planarity, suggesting geometric strain of the ester link is not important during catalysis. Several hydrogen atoms could be clearly identified and were included within the model. In keeping with a recent x-ray structure of subtilisin at 0.78 A (1), limited electron density is visible consistent with the putative location of a hydrogen atom approximately equidistant between the histidine and aspartate residues of the catalytic triad. Comparison of this high resolution crystal structure of the acyl-enzyme complex with that of native elastase at 1.1 A (2) showed that binding of the N-terminal part of the substrate can be accommodated with negligible structural rearrangements. In contrast, comparison with structures obtained as part of "time-resolved" studies on the reacting acyl-enzyme complex at >pH 7 (3) indicate small but significant structural differences, consistent with the proposed synchronization of ester hydrolysis and substrate release.

X-ray structure of a serine protease acyl-enzyme complex at 0.95-A resolution.,Katona G, Wilmouth RC, Wright PA, Berglund GI, Hajdu J, Neutze R, Schofield CJ J Biol Chem. 2002 Jun 14;277(24):21962-70. Epub 2002 Mar 14. PMID:11896054^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Katona G, Wilmouth RC, Wright PA, Berglund GI, Hajdu J, Neutze R, Schofield CJ. X-ray structure of a serine protease acyl-enzyme complex at 0.95-A resolution. J Biol Chem. 2002 Jun 14;277(24):21962-70. Epub 2002 Mar 14. PMID:11896054 doi:10.1074/jbc.M200676200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gvk"

@@ Line 1: / Line 1: @@
 ==Porcine pancreatic elastase acyl enzyme at 0.95 A resolution==
 <StructureSection load='1gvk' size='340' side='right' caption='[[1gvk]], [[Resolution|resolution]] 0.94&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0e|1b0e]], [[1bma|1bma]], [[1btu|1btu]], [[1c1m|1c1m]], [[1e34|1e34]], [[1e35|1e35]], [[1e36|1e36]], [[1e37|1e37]], [[1e38|1e38]], [[1e9h|1e9h]], [[1eai|1eai]], [[1eas|1eas]], [[1eat|1eat]], [[1eau|1eau]], [[1ela|1ela]], [[1elb|1elb]], [[1elc|1elc]], [[1eld|1eld]], [[1ele|1ele]], [[1elf|1elf]], [[1elg|1elg]], [[1esa|1esa]], [[1esb|1esb]], [[1est|1est]], [[1fle|1fle]], [[1fzz|1fzz]], [[1h9l|1h9l]], [[1hax|1hax]], [[1hay|1hay]], [[1haz|1haz]], [[1hb0|1hb0]], [[1hv7|1hv7]], [[1inc|1inc]], [[1jim|1jim]], [[1lvy|1lvy]], [[1nes|1nes]], [[1qgf|1qgf]], [[1qix|1qix]], [[1qnj|1qnj]], [[1qr3|1qr3]], [[2est|2est]], [[3est|3est]], [[4est|4est]], [[5est|5est]], [[6est|6est]], [[7est|7est]], [[8est|8est]], [[9est|9est]]</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=1gvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gvk OCA], [http://pdbe.org/1gvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gvk RCSB], [http://www.ebi.ac.uk/pdbsum/1gvk 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=1gvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gvk OCA], [http://pdbe.org/1gvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gvk RCSB], [http://www.ebi.ac.uk/pdbsum/1gvk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gvk ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
     <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].
+</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=1gvk ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1gvk

From Proteopedia

Revision as of 04:44, 21 September 2017

Porcine pancreatic elastase acyl enzyme at 0.95 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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