2agi
From Proteopedia
(New page: 200px<br /><applet load="2agi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2agi, resolution 1.140Å" /> '''The leupeptin-tryps...) |
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| - | [[Image:2agi.gif|left|200px]]<br /><applet load="2agi" size=" | + | [[Image:2agi.gif|left|200px]]<br /><applet load="2agi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2agi, resolution 1.140Å" /> | caption="2agi, resolution 1.140Å" /> | ||
'''The leupeptin-trypsin covalent complex at 1.14 A resolution'''<br /> | '''The leupeptin-trypsin covalent complex at 1.14 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral | + | Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of this classic serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 2AGI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4, CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http:// | + | 2AGI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
| - | [[Category: Jr., D | + | [[Category: Jr., D E.Koshland.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J M.]] |
| - | [[Category: Lu, C | + | [[Category: Lu, C J.]] |
| - | [[Category: Radisky, E | + | [[Category: Radisky, E S.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: acyl-enzyme; serine protease; proteinase; peptidase; hydrolase]] | [[Category: acyl-enzyme; serine protease; proteinase; peptidase; hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:10 2008'' |
Revision as of 14:27, 21 February 2008
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The leupeptin-trypsin covalent complex at 1.14 A resolution
Overview
Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of this classic serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction.
About this Structure
2AGI is a Single protein structure of sequence from Bos taurus with , and as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates., Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277
Page seeded by OCA on Thu Feb 21 16:27:10 2008
