1spb: Difference between revisions

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[[Image:1spb.gif|left|200px]]
{{Seed}}
[[Image:1spb.png|left|200px]]


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{{STRUCTURE_1spb|  PDB=1spb  |  SCENE=  }}  
{{STRUCTURE_1spb|  PDB=1spb  |  SCENE=  }}  


'''SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C'''
===SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C===




==Overview==
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BACKGROUND: The folding of the bacterial protease subtilisin BPN' (SBT) is dependent on its 77-residue prosegment, which is then autocatalytically removed to give the mature enzyme. Mature subtilisin represents a class of proteins that lacks an efficient folding pathway. Refolding of mature SBT is extremely slow unless catalyzed by the independently expressed prosegment, leading to a bimolecular complex. RESULTS: We report the crystal structure at 2.0 A resolution of the prosegment-SBT complex and consider its implications for prosubtilisin BPN' maturation and folding catalysis. The prosegment forms a compact domain that binds SBT through an extensive interface involving the enzyme's two parallel surface helices (residues 104-116 and 133-144), supplying negatively charged caps to the N termini of these helices. The prosegment C terminus binds in the enzyme active site in a product-like manner, with Tyr77 in the P1 binding pocket. CONCLUSIONS: The structure of the complex supports a unimolecular mechanism for prosubtilisin cleavage, involving a 25 A rearrangement of the SBT N terminus in a late folding step. A mechanism of folding catalysis in which the two helices and their connecting beta strand form a prosegment-stabilized folding nucleus is proposed. While this putative nucleus is stabilized by prosegment binding, the N-terminal and C-terminal subdomains of SBT could fold by propagation.
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{{ABSTRACT_PUBMED_8535784}}


==About this Structure==
==About this Structure==
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[[Category: Folding catalyst]]
[[Category: Folding catalyst]]
[[Category: Propeptide]]
[[Category: Propeptide]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:58:52 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:18:49 2008''

Revision as of 05:18, 28 July 2008

File:1spb.png

Template:STRUCTURE 1spb

SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C

Template:ABSTRACT PUBMED 8535784

About this Structure

1SPB is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'., Gallagher T, Gilliland G, Wang L, Bryan P, Structure. 1995 Sep 15;3(9):907-14. PMID:8535784

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