2pkc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2pkc.jpg|left|200px]] | [[Image:2pkc.jpg|left|200px]] | ||
'''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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 21: | Line 30: | ||
[[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
| |||||||||||||
| 2pkc, resolution 1.5Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | NA | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 18:14:04 2008
