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2e1p

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[[Image:2e1p.jpg|left|200px]]<br /><applet load="2e1p" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2e1p.jpg|left|200px]]
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caption="2e1p, resolution 2.30&Aring;" />
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'''Crystal structure of pro-Tk-subtilisin'''<br />
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{{Structure
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|PDB= 2e1p |SIZE=350|CAPTION= <scene name='initialview01'>2e1p</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|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]
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|GENE=
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}}
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'''Crystal structure of pro-Tk-subtilisin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2E1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E1P OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17237225 17237225]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:04:55 2008''
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''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


PDB ID 2e1p

Drag the structure with the mouse to rotate
, resolution 2.30Å
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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