1trm
From Proteopedia
(New page: 200px<br /><applet load="1trm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1trm, resolution 2.3Å" /> '''THE THREE-DIMENSIONAL...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1trm.gif|left|200px]]<br /><applet load="1trm" size=" | + | [[Image:1trm.gif|left|200px]]<br /><applet load="1trm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1trm, resolution 2.3Å" /> | caption="1trm, resolution 2.3Å" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the Asn102 mutant of trypsin was determined in order to | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and BEN 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:// | + | 1TRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=BEN:'>BEN</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=1TRM OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
| - | [[Category: Fletterick, R | + | [[Category: Fletterick, R J.]] |
[[Category: Sprang, S.]] | [[Category: Sprang, S.]] | ||
[[Category: Standing, T.]] | [[Category: Standing, T.]] | ||
| Line 21: | Line 21: | ||
[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:44 2008'' |
Revision as of 13:16, 21 February 2008
|
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.
About this Structure
1TRM is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis., Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS, Science. 1987 Aug 21;237(4817):905-9. PMID:3112942
Page seeded by OCA on Thu Feb 21 15:16:44 2008
