1y3g

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[[Image:1y3g.gif|left|200px]]<br /><applet load="1y3g" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y3g.gif|left|200px]]
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caption="1y3g, resolution 2.10&Aring;" />
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'''Crystal Structure of a Silanediol Protease Inhibitor Bound to Thermolysin'''<br />
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{{Structure
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|PDB= 1y3g |SIZE=350|CAPTION= <scene name='initialview01'>1y3g</scene>, resolution 2.10&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene> and <scene name='pdbligand=3PL:3-PHENYLPROPANAL'>3PL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27]
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|GENE=
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}}
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'''Crystal Structure of a Silanediol Protease Inhibitor Bound to Thermolysin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Y3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=DMS:'>DMS</scene> and <scene name='pdbligand=3PL:'>3PL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y3G OCA].
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1Y3G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y3G OCA].
==Reference==
==Reference==
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Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin., Juers DH, Kim J, Matthews BW, Sieburth SM, Biochemistry. 2005 Dec 20;44(50):16524-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16342943 16342943]
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Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin., Juers DH, Kim J, Matthews BW, Sieburth SM, Biochemistry. 2005 Dec 20;44(50):16524-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16342943 16342943]
[[Category: Bacillus thermoproteolyticus]]
[[Category: Bacillus thermoproteolyticus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thermolysin]]
[[Category: thermolysin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:17:58 2008''

Revision as of 13:17, 20 March 2008


PDB ID 1y3g

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: , , and
Activity: Thermolysin, with EC number 3.4.24.27
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of a Silanediol Protease Inhibitor Bound to Thermolysin


Overview

Dialkylsilanediols have been found to be an effective functional group for the design of active-site-directed protease inhibitors, including aspartic (HIV protease) and metallo (ACE and thermolysin) proteases. The use of silanediols is predicated on its resemblance to the hydrated carbonyl transition-state structure of amide hydrolysis. This concept has been tested by replacing the presumed tetrahedral carbon of a thermolysin substrate with a silanediol group, resulting in an inhibitor with an inhibition constant K(i) = 40 nM. The structure of the silanediol bound to the active site of thermolysin was found to have a conformation very similar to that of a corresponding phosphonamidate inhibitor (K(i) = 10 nM). In both cases, a single oxygen is within bonding distance to the active-site zinc ion, mimicking the presumed tetrahedral transition state. There are binding differences that appear to be related to the presence or absence of protons on the oxygens attached to the silicon or phosphorus. This is the first crystal structure of an organosilane bound to the active site of a protease.

About this Structure

1Y3G is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.

Reference

Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin., Juers DH, Kim J, Matthews BW, Sieburth SM, Biochemistry. 2005 Dec 20;44(50):16524-8. PMID:16342943

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