1elg
From Proteopedia
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| - | [[Image:1elg.gif|left|200px]] | + | [[Image:1elg.gif|left|200px]] |
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| - | '''NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH''' | + | {{Structure |
| + | |PDB= 1elg |SIZE=350|CAPTION= <scene name='initialview01'>1elg</scene>, resolution 1.65Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=BAA:(TERT-BUTYLOXYCARBONYL)-ALANYL-ALANYL-AMINE'>BAA</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ELG is a [ | + | 1ELG is a [[Single protein]] structure of 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=1ELG OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7779821 7779821] |
[[Category: Pancreatic elastase]] | [[Category: Pancreatic elastase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: complex (hydrolase/inhibitor)]] | [[Category: complex (hydrolase/inhibitor)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:57:11 2008'' |
Revision as of 08:57, 20 March 2008
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| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH
Overview
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.
About this Structure
1ELG is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 10:57:11 2008
