2e1p
From Proteopedia
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| - | [[Image:2e1p.jpg|left|200px]] | + | [[Image:2e1p.jpg|left|200px]] |
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| - | '''Crystal structure of pro-Tk-subtilisin''' | + | {{Structure |
| + | |PDB= 2e1p |SIZE=350|CAPTION= <scene name='initialview01'>2e1p</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of pro-Tk-subtilisin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2E1P is a [ | + | 2E1P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E1P OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+-induced folding., Tanaka S, Saito K, Chon H, Matsumura H, Koga Y, Takano K, Kanaya S, J Biol Chem. 2007 Mar 16;282(11):8246-55. Epub 2007 Jan 19. PMID:[http:// | + | Crystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+-induced folding., Tanaka S, Saito K, Chon H, Matsumura H, Koga Y, Takano K, Kanaya S, J Biol Chem. 2007 Mar 16;282(11):8246-55. Epub 2007 Jan 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17237225 17237225] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Subtilisin]] | [[Category: Subtilisin]] | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''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 16:34:06 2008'' |
Revision as of 14:34, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | |||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of pro-Tk-subtilisin
Overview
The crystal structure of an active site mutant of pro-Tk-subtilisin (pro-S324A) from the hyperthermophilic archaeon Thermococcus kodakaraensis was determined at 2.3 A resolution. The overall structure of this protein is similar to those of bacterial subtilisin-propeptide complexes, except that the peptide bond linking the propeptide and mature domain contacts with the active site, and the mature domain contains six Ca2+ binding sites. The Ca-1 site is conserved in bacterial subtilisins but is formed prior to autoprocessing, unlike the corresponding sites of bacterial subtilisins. All other Ca2+-binding sites are unique in the pro-S324A structure and are located at the surface loops. Four of them apparently contribute to the stability of the central alphabetaalpha substructure of the mature domain. The CD spectra, 1-anilino-8-naphthalenesulfonic acid fluorescence spectra, and sensitivities to chymotryptic digestion of this protein indicate that the conformation of pro-S324A is changed from an unstable molten globule-like structure to a stable native one upon Ca2+ binding. Another active site mutant, pro-S324C, was shown to be autoprocessed to form a propeptide-mature domain complex in the presence of Ca2+. The CD spectra of this protein indicate that the structure of pro-S324C is changed upon Ca2+ binding like pro-S324A but is not seriously changed upon subsequent autoprocessing. These results suggest that the maturation process of Tk-subtilisin is different from that of bacterial subtilisins in terms of the requirement of Ca2+ for folding of the mature domain and completion of the folding process prior to autoprocessing.
About this Structure
2E1P is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.
Reference
Crystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+-induced folding., Tanaka S, Saito K, Chon H, Matsumura H, Koga Y, Takano K, Kanaya S, J Biol Chem. 2007 Mar 16;282(11):8246-55. Epub 2007 Jan 19. PMID:17237225
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