2trm: Difference between revisions

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[[Image:2trm.~~jpg~~|left|200px]]

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

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~~'''~~THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS~~'''~~

===THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS===

~~==Overview==~~

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The ~~structure of~~ the ~~Asn102 mutant of trypsin was determined in order~~ to ~~distinguish whether~~ the ~~reduced activity of the mutant~~ at ~~neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine~~. ~~The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole~~, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is ~~unable to accept~~ the ~~serine hydroxyl proton~~.

The line below this paragraph, {{ABSTRACT_PUBMED_3112942}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 3112942 is the PubMed ID number.

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==About this Structure==

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[[Category: Finer-Moore, J.]]

[[Category: Stroud, R M.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 17~~:26:21 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:58:06 2008''

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-[[Image:2trm.jpg|left|200px]]
+{{Seed}}
+[[Image:2trm.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2trm|  PDB=2trm  |  SCENE=  }}
-'''THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS'''
+===THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS===
-==Overview==
+<!--
-The structure of the Asn102 mutant of trypsin was determined in order to distinguish whether the reduced activity of the mutant at neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine. The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton.
+The line below this paragraph, {{ABSTRACT_PUBMED_3112942}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 3112942 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_3112942}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Finer-Moore, J.]]
 [[Category: Stroud, R M.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:26:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:58:06 2008''