1ptk: Difference between revisions
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[[Image:1ptk.jpg|left|200px]] | [[Image:1ptk.jpg|left|200px]] | ||
'''STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K''' | {{Structure | ||
|PDB= 1ptk |SIZE=350|CAPTION= <scene name='initialview01'>1ptk</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</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] | |||
|GENE= | |||
}} | |||
'''STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PTK is a [ | 1PTK 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=1PTK OCA]. | ||
==Reference== | ==Reference== | ||
Studies on the inhibitory action of mercury upon proteinase K., Muller A, Saenger W, J Biol Chem. 1993 Dec 15;268(35):26150-4. PMID:[http:// | Studies on the inhibitory action of mercury upon proteinase K., Muller A, Saenger W, J Biol Chem. 1993 Dec 15;268(35):26150-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8253733 8253733] | ||
[[Category: Engyodontium album]] | [[Category: Engyodontium album]] | ||
[[Category: Peptidase K]] | [[Category: Peptidase K]] | ||
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[[Category: hydrolase(serine proteinase)]] | [[Category: hydrolase(serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:53 2008'' |
Revision as of 14:28, 20 March 2008
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, resolution 2.4Å | |||||||
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Ligands: | and | ||||||
Activity: | Peptidase K, with EC number 3.4.21.64 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K
OverviewOverview
In proteinase K, Cys73 is located "below" the imidazole of the active site His69. In a 2.4-A resolution x-ray crystal structure of the complex formed between the enzyme and HgAc2, two Hg(II) positions are found: a fully occupied site, covalently bound to Cys73 (S gamma), which disrupts the catalytic triad (Asp39-His69-Ser224), and a 2-fold disordered (25 and 35% occupancy), noncovalent complexation to His72, Cys73, and Thr76 of lower affinity. The enzyme is inhibited noncompetitively at low concentrations and competitively above stoichiometric concentrations of Hg(II), but it retains 7% residual activity. This can be rationalized if the molecule is flexible enough to permit transient formation of the catalytic triad. Except for the active site, only minor structural changes are observed upon binding of Hg(II), but the thermal stability is reduced by 4 degrees C.
About this StructureAbout this Structure
1PTK is a Single protein structure of sequence from Engyodontium album. Full crystallographic information is available from OCA.
ReferenceReference
Studies on the inhibitory action of mercury upon proteinase K., Muller A, Saenger W, J Biol Chem. 1993 Dec 15;268(35):26150-4. PMID:8253733
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