2age: Difference between revisions

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[[Image:2age.~~gif~~|left|200px]]

[[Image:2age.png|left|200px]]

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~~'''~~Succinyl-AAPR-trypsin acyl-enzyme at 1.15 A resolution~~'''~~

===Succinyl-AAPR-trypsin acyl-enzyme at 1.15 A resolution===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_16636277}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16636277 is the PubMed ID number.

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==About this Structure==

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[[Category: Proteinase]]

[[Category: Serine protease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 19~~:01:03 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:00:38 2008''

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-[[Image:2age.gif|left|200px]]
+{{Seed}}
+[[Image:2age.png|left|200px]]
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 {{STRUCTURE_2age|  PDB=2age  |  SCENE=  }}
-'''Succinyl-AAPR-trypsin acyl-enzyme at 1.15 A resolution'''
+===Succinyl-AAPR-trypsin acyl-enzyme at 1.15 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16636277}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16636277 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16636277}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Proteinase]]
 [[Category: Serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:01:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:00:38 2008''