2deo: Difference between revisions

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[[Image:2deo.gif|left|200px]]
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{{STRUCTURE_2deo|  PDB=2deo  |  SCENE=  }}  
{{STRUCTURE_2deo|  PDB=2deo  |  SCENE=  }}  


'''1510-N membrane protease specific for a stomatin homolog from Pyrococcus horikoshii'''
===1510-N membrane protease specific for a stomatin homolog from Pyrococcus horikoshii===




==Overview==
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Membrane-bound proteases are involved in various regulatory functions. Our previous study indicated that the N-terminal region of an open reading frame, PH1510 (residues 16-236, designated as 1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii, is a serine protease with a catalytic Ser-Lys dyad that specifically cleaves the C-terminal hydrophobic residues of a membrane protein, the stomatin-homolog PH1511. In humans, an absence of stomatin is associated with a form of hemolytic anemia known as hereditary stomatocytosis, but the function of stomatin is not fully understood. Here, we report the crystal structure of 1510-N in dimeric form. Each active site of 1510-N is rich in hydrophobic residues, which accounts for the substrate-specificity. The monomer of 1510-N shows structural similarity to one monomer of Escherichia coli ClpP, an ATP-dependent tetradecameric protease. But, their oligomeric forms are different. Major contributors to dimeric interaction in 1510-N are the alpha7 helix and beta9 strand, both of which are missing from ClpP. While the long handle region of ClpP contributes to the stacking of two heptameric rings, the corresponding L2 loop of 1510-N is disordered because the region has little interaction with other residues of the same molecule. The catalytic Ser97 of 1510-N is in almost the same location as the catalytic Ser97 of E.coli ClpP, whereas another residue, Lys138, presumably forming the catalytic dyad, is located in the disordered L2 region of 1510-N. These findings suggest that the binding of the substrate to the catalytic site of 1510-N induces conformational changes in a region that includes loop L2 so that Lys138 approaches the catalytic Ser97.
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{{ABSTRACT_PUBMED_16574150}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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]
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]
A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii., Yokoyama H, Matsui I, J Biol Chem. 2005 Feb 25;280(8):6588-94. Epub 2004 Dec 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15611110 15611110]
[[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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Revision as of 16:17, 28 July 2008

File:2deo.png

Template:STRUCTURE 2deo

1510-N membrane protease specific for a stomatin homolog from Pyrococcus horikoshii1510-N membrane protease specific for a stomatin homolog from Pyrococcus horikoshii

Template:ABSTRACT PUBMED 16574150

About this StructureAbout this Structure

2DEO is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

ReferenceReference

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

A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii., Yokoyama H, Matsui I, J Biol Chem. 2005 Feb 25;280(8):6588-94. Epub 2004 Dec 16. PMID:15611110

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