2pkc
From Proteopedia
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| - | [[Image:2pkc.jpg|left|200px]] | + | [[Image:2pkc.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 2pkc |SIZE=350|CAPTION= <scene name='initialview01'>2pkc</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</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= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PKC is a [ | + | 2PKC 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=2PKC OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of calcium-free proteinase K at 1.5-A resolution., Muller A, Hinrichs W, Wolf WM, Saenger W, J Biol Chem. 1994 Sep 16;269(37):23108-11. PMID:[http:// | + | Crystal structure of calcium-free proteinase K at 1.5-A resolution., Muller A, Hinrichs W, Wolf WM, Saenger W, J Biol Chem. 1994 Sep 16;269(37):23108-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8083213 8083213] |
[[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 18:14:04 2008'' |
Revision as of 16:14, 20 March 2008
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| , resolution 1.5Å | |||||||
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| Ligands: | |||||||
| Activity: | Peptidase K, with EC number 3.4.21.64 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION
Overview
Proteinase K from the fungus Tritirachium album Limber binds two Ca2+ ions, one strongly (Ca 1) and the other weakly (Ca 2). Removal of these cations reduces the stability of proteinase K as shown by thermal denaturation, but the proteolytic activity is unchanged. The x-ray structures of native and Ca(2+)-free proteinase K at 1.5-A resolution show that there are no cuts in the polypeptide backbone (i.e. no autolysis), Ca 1 has been replaced by Na+, while Ca 2 has been substituted by a water associated with a larger but locally confined structural change at that site. A small but concerted geometrical shift is transmitted from the Ca 1 site via eight secondary structure elements to the substrate recognition site (Gly100-Tyr104, and Ser132-Gly136) but not to the catalytic triad (Asp39,His69,Ser224). This is accompanied by positional changes of localized waters.
About this Structure
2PKC is a Single protein structure of sequence from Engyodontium album. Full crystallographic information is available from OCA.
Reference
Crystal structure of calcium-free proteinase K at 1.5-A resolution., Muller A, Hinrichs W, Wolf WM, Saenger W, J Biol Chem. 1994 Sep 16;269(37):23108-11. PMID:8083213
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