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| - | [[Image:1pj8.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1pj8| PDB=1pj8 | SCENE= }} | | {{STRUCTURE_1pj8| PDB=1pj8 | SCENE= }} |
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| - | '''Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution'''
| + | ===Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8811735}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8811735 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8811735}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Structure]] | | [[Category: Structure]] |
| | [[Category: Ternary complex]] | | [[Category: Ternary complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:08:36 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:55:32 2008'' |
Revision as of 01:55, 28 July 2008
Template:STRUCTURE 1pj8
Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution
Template:ABSTRACT PUBMED 8811735
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
Page seeded by OCA on Mon Jul 28 04:55:32 2008
