1elf

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[[Image:1elf.gif|left|200px]]<br /><applet load="1elf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1elf.gif|left|200px]]
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caption="1elf, resolution 1.7&Aring;" />
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'''NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH'''<br />
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{{Structure
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|PDB= 1elf |SIZE=350|CAPTION= <scene name='initialview01'>1elf</scene>, resolution 1.7&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=BAF:(TERT-BUTYLOXYCARBONYL)-ALANYL-AMINO ETHYL-FORMAMIDE'>BAF</scene>
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|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]
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|GENE=
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}}
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'''NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ELF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BAF:'>BAF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELF OCA].
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1ELF 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=1ELF OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7779821 7779821]
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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)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:57:16 2008''

Revision as of 08:57, 20 March 2008


PDB ID 1elf

Drag the structure with the mouse to rotate
, resolution 1.7Å
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

1ELF 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

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