2nr9
From Proteopedia
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|PDB= 2nr9 |SIZE=350|CAPTION= <scene name='initialview01'>2nr9</scene>, resolution 2.20Å | |PDB= 2nr9 |SIZE=350|CAPTION= <scene name='initialview01'>2nr9</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PA6:(R)-2-(FORMYLOXY)-3-(PHOSPHONOOXY)PROPYL+PENTANOATE'>PA6</scene> | + | |LIGAND= <scene name='pdbligand=PA6:(R)-2-(FORMYLOXY)-3-(PHOSPHONOOXY)PROPYL+PENTANOATE'>PA6</scene>, <scene name='pdbligand=PQE:3,6,12,15,18,21,24-HEPTAOXAHEXATRIACONTAN-1-OL'>PQE</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= glpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | |GENE= glpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2ic8|2IC8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nr9 OCA], [http://www.ebi.ac.uk/pdbsum/2nr9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nr9 RCSB]</span> | ||
}} | }} | ||
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[[Category: James, M N.G.]] | [[Category: James, M N.G.]] | ||
[[Category: Lemieux, M J.]] | [[Category: Lemieux, M J.]] | ||
| - | [[Category: PA6]] | ||
| - | [[Category: PQE]] | ||
[[Category: intramembrane peptidase]] | [[Category: intramembrane peptidase]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:07:08 2008'' |
Revision as of 01:07, 31 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | glpG (Haemophilus influenzae) | ||||||
| Activity: | Rhomboid protease, with EC number 3.4.21.105 | ||||||
| Related: | 2IC8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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