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| | {{STRUCTURE_2e1p| PDB=2e1p | SCENE= }} | | {{STRUCTURE_2e1p| PDB=2e1p | SCENE= }} |
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| - | '''Crystal structure of pro-Tk-subtilisin'''
| + | ===Crystal structure of pro-Tk-subtilisin=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17237225}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17237225 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17237225}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Serine protease]] | | [[Category: Serine protease]] |
| | [[Category: Subtilisin]] | | [[Category: Subtilisin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:45:28 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:44:54 2008'' |
Revision as of 11:45, 29 July 2008
Template:STRUCTURE 2e1p
Crystal structure of pro-Tk-subtilisin
Template:ABSTRACT PUBMED 17237225
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
Page seeded by OCA on Tue Jul 29 14:44:54 2008
