1pj8
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1pj8 |SIZE=350|CAPTION= <scene name='initialview01'>1pj8</scene>, resolution 2.2Å | |PDB= 1pj8 |SIZE=350|CAPTION= <scene name='initialview01'>1pj8</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pj8 OCA], [http://www.ebi.ac.uk/pdbsum/1pj8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pj8 RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Visanji, M.]] | [[Category: Visanji, M.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
| - | [[Category: HG]] | ||
| - | [[Category: NH2]] | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
[[Category: mercury]] | [[Category: mercury]] | ||
| Line 38: | Line 39: | ||
[[Category: ternary complex]] | [[Category: ternary complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:22 2008'' |
Revision as of 20:00, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Peptidase K, with EC number 3.4.21.64 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 23:00:22 2008
