2trm

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[[Image:2trm.jpg|left|200px]]<br /><applet load="2trm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2trm.jpg|left|200px]]
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caption="2trm, resolution 2.8&Aring;" />
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'''THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS'''<br />
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{{Structure
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|PDB= 2trm |SIZE=350|CAPTION= <scene name='initialview01'>2trm</scene>, resolution 2.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2TRM 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=2TRM OCA].
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2TRM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TRM OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3112942 3112942]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/3112942 3112942]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase (serine proteinase)]]
[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:39:23 2008''

Revision as of 16:39, 20 March 2008


PDB ID 2trm

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands: and
Activity: Trypsin, with EC number 3.4.21.4
Coordinates: save as pdb, mmCIF, xml



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

2TRM is a Single protein structure of sequence from Rattus norvegicus. 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

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