2nr9
From Proteopedia
(New page: 200px<br /><applet load="2nr9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nr9, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:2nr9.gif|left|200px]]<br /><applet load="2nr9" size=" | + | [[Image:2nr9.gif|left|200px]]<br /><applet load="2nr9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2nr9, resolution 2.20Å" /> | caption="2nr9, resolution 2.20Å" /> | ||
'''Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae'''<br /> | '''Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rhomboid peptidases are members of a family of regulated intramembrane | + | Rhomboid peptidases are members of a family of regulated intramembrane peptidases that cleave the transmembrane segments of integral membrane proteins. Rhomboid peptidases have been shown to play a major role in developmental processes in Drosophila and in mitochondrial maintenance in yeast. Most recently, the function of rhomboid peptidases has been directly linked to apoptosis. We have solved the structure of the rhomboid peptidase from Haemophilus influenzae (hiGlpG) to 2.2-A resolution. The phasing for the crystals of hiGlpG was provided mainly by molecular replacement, by using the coordinates of the Escherichia coli rhomboid (ecGlpG). The structural results on these rhomboid peptidases have allowed us to speculate on the catalytic mechanism of substrate cleavage in a membranous environment. We have identified the relative disposition of the nucleophilic serine to the general base/acid function of the conserved histidine. Modeling a tetrapeptide substrate in the context of the rhomboid structure reveals an oxyanion hole comprising the side chain of a second conserved histidine and the main-chain NH of the nucleophilic serine residue. In both hiGlpG and ecGlpG structures, a water molecule occupies this oxyanion hole. |
==About this Structure== | ==About this Structure== | ||
| - | 2NR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with PA6 and PQE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.105 3.4.21.105] Full crystallographic information is available from [http:// | + | 2NR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=PA6:'>PA6</scene> and <scene name='pdbligand=PQE:'>PQE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Rhomboid_protease Rhomboid protease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.105 3.4.21.105] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NR9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rhomboid protease]] | [[Category: Rhomboid protease]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bateman, K | + | [[Category: Bateman, K S.]] |
| - | [[Category: Cherney, M | + | [[Category: Cherney, M M.]] |
| - | [[Category: Fischer, S | + | [[Category: Fischer, S J.]] |
| - | [[Category: James, M | + | [[Category: James, M N.G.]] |
| - | [[Category: Lemieux, M | + | [[Category: Lemieux, M J.]] |
[[Category: PA6]] | [[Category: PA6]] | ||
[[Category: PQE]] | [[Category: PQE]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:00 2008'' |
Revision as of 16:10, 21 February 2008
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Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae
Overview
Rhomboid peptidases are members of a family of regulated intramembrane peptidases that cleave the transmembrane segments of integral membrane proteins. Rhomboid peptidases have been shown to play a major role in developmental processes in Drosophila and in mitochondrial maintenance in yeast. Most recently, the function of rhomboid peptidases has been directly linked to apoptosis. We have solved the structure of the rhomboid peptidase from Haemophilus influenzae (hiGlpG) to 2.2-A resolution. The phasing for the crystals of hiGlpG was provided mainly by molecular replacement, by using the coordinates of the Escherichia coli rhomboid (ecGlpG). The structural results on these rhomboid peptidases have allowed us to speculate on the catalytic mechanism of substrate cleavage in a membranous environment. We have identified the relative disposition of the nucleophilic serine to the general base/acid function of the conserved histidine. Modeling a tetrapeptide substrate in the context of the rhomboid structure reveals an oxyanion hole comprising the side chain of a second conserved histidine and the main-chain NH of the nucleophilic serine residue. In both hiGlpG and ecGlpG structures, a water molecule occupies this oxyanion hole.
About this Structure
2NR9 is a Single protein structure of sequence from Haemophilus influenzae with and as ligands. Active as Rhomboid protease, with EC number 3.4.21.105 Full crystallographic information is available from OCA.
Reference
The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis., Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, James MN, Proc Natl Acad Sci U S A. 2007 Jan 16;104(3):750-4. Epub 2007 Jan 8. PMID:17210913
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