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1pj8

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[[Image:1pj8.gif|left|200px]]<br /><applet load="1pj8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pj8.gif|left|200px]]
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caption="1pj8, resolution 2.2&Aring;" />
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'''Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution'''<br />
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{{Structure
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|PDB= 1pj8 |SIZE=350|CAPTION= <scene name='initialview01'>1pj8</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64]
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|GENE=
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}}
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'''Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PJ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJ8 OCA].
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1PJ8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJ8 OCA].
==Reference==
==Reference==
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Structure of a ternary complex of proteinase K, mercury, and a substrate-analogue hexa-peptide at 2.2 A resolution., Saxena AK, Singh TP, Peters K, Fittkau S, Visanji M, Wilson KS, Betzel C, Proteins. 1996 Jun;25(2):195-201. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8811735 8811735]
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Structure of a ternary complex of proteinase K, mercury, and a substrate-analogue hexa-peptide at 2.2 A resolution., Saxena AK, Singh TP, Peters K, Fittkau S, Visanji M, Wilson KS, Betzel C, Proteins. 1996 Jun;25(2):195-201. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8811735 8811735]
[[Category: Engyodontium album]]
[[Category: Engyodontium album]]
[[Category: Peptidase K]]
[[Category: Peptidase K]]
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[[Category: ternary complex]]
[[Category: ternary complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:25:04 2008''

Revision as of 11:25, 20 March 2008

Image:1pj8.gif


PDB ID 1pj8

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: and
Activity: Peptidase K, with EC number 3.4.21.64
Coordinates: save as pdb, mmCIF, xml



Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution


Overview

The crystal structure of a ternary complex of proteinase K, Hg(II) and a hexapeptide N-Ac-Pro-Ala-Pro-Phe-Pro-Ala-NH2 has been determined at 2.2 A resolution and refined to an R factor of 0.172 for 12,910 reflections. The mercury atom occupies two alternate sites, each of which was assigned an occupancy of 0.45. These two sites are bridged by Cys-73 S gamma which forms covalent bonds to both. Both mercury sites form regular polyhedrons involving atoms from residues Asp-39, His-69, Cys-73, His-72, Met-225, and Wat-324. The complex formation with mercury seems to disturb the stereochemistry of the residues of the catalytic triad Asp-39, His-69, and Ser-224 appreciably, thus reducing the enzymatic activity of proteinase K to 15%. The electron density in the difference Fourier map shows that the hexapeptide occupies the S1 subsite predominantly and the standard recognition site constituted by Ser-132 to Gly-136 and Gly-100 to Tyr-104 segments is virtually empty. The hexapeptide is held firmly through a series of hydrogen bonds involving protein atoms and water molecules. As a result of complex formation, Asp-39, His-69, Met-225, Ile-220, Ser-219, Thr-223, and Ser-224 residues move appreciably to accommodate the mercury atoms and the hexapeptide. The largest movement is observed for Met-225 which is involved in multiple interactions with both mercury and the hexapeptide. The activity results indicate an inhibition rate of 95%, as a result of the combined effect of mercury and hexapeptide.

About this Structure

1PJ8 is a Single protein structure of sequence from Engyodontium album. Full crystallographic information is available from OCA.

Reference

Structure of a ternary complex of proteinase K, mercury, and a substrate-analogue hexa-peptide at 2.2 A resolution., Saxena AK, Singh TP, Peters K, Fittkau S, Visanji M, Wilson KS, Betzel C, Proteins. 1996 Jun;25(2):195-201. PMID:8811735

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