2agi: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="2agi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2agi, resolution 1.140Å" /> '''The leupeptin-tryps...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2agi.gif|left|200px]]<br /><applet load="2agi" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2agi.gif|left|200px]]<br /><applet load="2agi" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2agi, resolution 1.140&Aring;" />
caption="2agi, resolution 1.140&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AGI OCA].  
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==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trypsin]]
[[Category: Trypsin]]
[[Category: Jr., D.E.Koshland.]]
[[Category: Jr., D E.Koshland.]]
[[Category: Lee, J.M.]]
[[Category: Lee, J M.]]
[[Category: Lu, C.J.]]
[[Category: Lu, C J.]]
[[Category: Radisky, E.S.]]
[[Category: Radisky, E S.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CA]]
[[Category: CA]]
Line 23: Line 23:
[[Category: acyl-enzyme; serine protease; proteinase; peptidase; hydrolase]]
[[Category: acyl-enzyme; serine protease; proteinase; peptidase; hydrolase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:06:26 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:10 2008''