2nr9

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[[Image:2nr9.gif|left|200px]]
 
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==Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae==
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The line below this paragraph, containing "STRUCTURE_2nr9", creates the "Structure Box" on the page.
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<StructureSection load='2nr9' size='340' side='right'caption='[[2nr9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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{{STRUCTURE_2nr9| PDB=2nr9 | SCENE= }}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLPG_HAEIN GLPG_HAEIN] Rhomboid-type serine protease that catalyzes intramembrane proteolysis (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nr/2nr9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae'''
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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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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2NR9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NR9 OCA].
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</div>
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<div class="pdbe-citations 2nr9" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17210913 17210913]
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*[[Rhomboid protease|Rhomboid protease]]
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[[Category: Haemophilus influenzae]]
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== References ==
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[[Category: Rhomboid protease]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Bateman, K S.]]
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</StructureSection>
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[[Category: Cherney, M M.]]
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[[Category: Haemophilus influenzae 86-028NP]]
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[[Category: Fischer, S J.]]
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[[Category: Large Structures]]
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[[Category: James, M N.G.]]
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[[Category: Bateman KS]]
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[[Category: Lemieux, M J.]]
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[[Category: Cherney MM]]
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[[Category: Intramembrane peptidase]]
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[[Category: Fischer SJ]]
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[[Category: Membrane protein]]
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[[Category: James MNG]]
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[[Category: Rhomboid protease]]
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[[Category: Lemieux MJ]]
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[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:48:50 2008''
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Current revision

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae

PDB ID 2nr9

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