3bpp

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{{STRUCTURE_3bpp| PDB=3bpp | SCENE= }}
{{STRUCTURE_3bpp| PDB=3bpp | SCENE= }}
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'''1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii'''
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===1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii===
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==Overview==
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Membrane-bound proteases are involved in various regulatory functions. A previous report indicates that the N-terminal region of PH1510 (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138), and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511. According to the crystal structure of the wild-type 1510-N in dimeric form, the active site around Ser97 is in a hydrophobic environment suitable for the hydrophobic substrates. This article reports the crystal structure of the K138A mutant of 1510-N at 2.3 A resolution. The determined structure contains one molecule per asymmetric unit, but 1510-N is active in dimeric form. Two possible sets of dimer were found from the symmetry-related molecules. One dimer is almost the same as the wild-type 1510-N. Another dimer is probably in an inactive form. The L2 loop, which is disordered in the wild-type structure, is significantly kinked at around A-138 in the K138A mutant. Thus Lys138 probably has an important role on the conformation of L2.
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{{ABSTRACT_PUBMED_18421152}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin., Yokoyama H, Hamamatsu S, Fujii S, Matsui I, J Synchrotron Radiat. 2008 May;15(Pt 3):254-7. Epub 2008 Apr 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18421152 18421152]
Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin., Yokoyama H, Hamamatsu S, Fujii S, Matsui I, J Synchrotron Radiat. 2008 May;15(Pt 3):254-7. Epub 2008 Apr 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18421152 18421152]
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Molecular structure of a novel membrane protease specific for a stomatin homolog from the hyperthermophilic archaeon Pyrococcus horikoshii., Yokoyama H, Matsui E, Akiba T, Harata K, Matsui I, J Mol Biol. 2006 May 12;358(4):1152-64. Epub 2006 Mar 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16574150 16574150]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Specific for a stomatin homolog]]
[[Category: Specific for a stomatin homolog]]
[[Category: Thermostable]]
[[Category: Thermostable]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:33:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:53:20 2008''

Revision as of 10:53, 29 July 2008

Image:3bpp.png

Template:STRUCTURE 3bpp

1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii

Template:ABSTRACT PUBMED 18421152

About this Structure

3BPP is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin., Yokoyama H, Hamamatsu S, Fujii S, Matsui I, J Synchrotron Radiat. 2008 May;15(Pt 3):254-7. Epub 2008 Apr 18. PMID:18421152

Molecular structure of a novel membrane protease specific for a stomatin homolog from the hyperthermophilic archaeon Pyrococcus horikoshii., Yokoyama H, Matsui E, Akiba T, Harata K, Matsui I, J Mol Biol. 2006 May 12;358(4):1152-64. Epub 2006 Mar 9. PMID:16574150

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