1hax

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[[Image:1hax.gif|left|200px]]<br /><applet load="1hax" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hax.gif|left|200px]]
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caption="1hax, resolution 1.6&Aring;" />
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'''SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (A) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 AT PH 5'''<br />
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{{Structure
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|PDB= 1hax |SIZE=350|CAPTION= <scene name='initialview01'>1hax</scene>, resolution 1.6&Aring;
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|SITE= <scene name='pdbsite=CAT:Active+Site+Catalytic+Triad'>CAT</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.4.21.36 Transferred entry: 3.4.21.36], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.11 3.4.21.11]
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|GENE=
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}}
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'''SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (A) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 AT PH 5'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1HAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.4.21.36 Transferred entry: 3.4.21.36], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.11 3.4.21.11] Known structural/functional Site: <scene name='pdbsite=CAT:Active+Site+Catalytic+Triad'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAX OCA].
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1HAX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HAX OCA].
==Reference==
==Reference==
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X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11473259 11473259]
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X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11473259 11473259]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: serine proteinase]]
[[Category: serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:38 2008''

Revision as of 09:34, 20 March 2008


PDB ID 1hax

Drag the structure with the mouse to rotate
, resolution 1.6Å
Sites:
Ligands: and
Activity: Transferred entry: 3.4.21.36, with EC number 3.4.21.11
Coordinates: save as pdb, mmCIF, xml



SNAPSHOTS OF SERINE PROTEASE CATALYSIS: (A) ACYL-ENZYME INTERMEDIATE BETWEEN PORCINE PANCREATIC ELASTASE AND HUMAN BETA-CASOMORPHIN-7 AT PH 5


Overview

Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues. An oxyanion hole, consisting of the peptide amide of the active site serine and a neighbouring glycine, was identified, and hydrogen bonding in the oxyanion hole was suggested to stabilize the two proposed tetrahedral intermediates on the catalytic pathway. Here we show electron density changes consistent with the formation of a tetrahedral intermediate during the hydrolysis of an acyl-enzyme complex formed between a natural heptapeptide and elastase. No electron density for an enzyme-product complex was observed. The structures also suggest a mechanism for the synchronization of hydrolysis and peptide release triggered by the conversion of the sp2 hybridized carbonyl carbon to an sp3 carbon in the tetrahedral intermediate. This affects the location of the peptide in the active site cleft, triggering the collapse of a hydrogen bonding network between the peptide and the beta-sheet of the active site.

About this Structure

1HAX is a Single protein structure of sequence from Homo sapiens and Sus scrofa. Full crystallographic information is available from OCA.

Reference

X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate., Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J, Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:11473259

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