2nr9
From Proteopedia
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(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="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2nr9, resolution 2.20Å" /> | ||
| - | '''Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae'''<br /> | ||
| - | == | + | ==Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae== |
| - | Rhomboid peptidases are members of a family of regulated intramembrane | + | <StructureSection load='2nr9' size='340' side='right'caption='[[2nr9]], [[Resolution|resolution]] 2.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2nr9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_86-028NP Haemophilus influenzae 86-028NP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NR9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nr9 OCA], [https://pdbe.org/2nr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nr9 RCSB], [https://www.ebi.ac.uk/pdbsum/2nr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nr9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GLPG_HAEIN GLPG_HAEIN] Rhomboid-type serine protease that catalyzes intramembrane proteolysis (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nr/2nr9_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nr9 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:17210913</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2nr9" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Rhomboid protease|Rhomboid protease]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Haemophilus influenzae 86-028NP]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bateman KS]] | ||
| + | [[Category: Cherney MM]] | ||
| + | [[Category: Fischer SJ]] | ||
| + | [[Category: James MNG]] | ||
| + | [[Category: Lemieux MJ]] | ||
Current revision
Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae
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