2nr9

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[[Image:2nr9.gif|left|200px]]
 
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{{Structure
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==Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae==
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|PDB= 2nr9 |SIZE=350|CAPTION= <scene name='initialview01'>2nr9</scene>, resolution 2.20&Aring;
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<StructureSection load='2nr9' size='340' side='right'caption='[[2nr9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PA6:(R)-2-(FORMYLOXY)-3-(PHOSPHONOOXY)PROPYL+PENTANOATE'>PA6</scene> and <scene name='pdbligand=PQE:3,6,12,15,18,21,24-HEPTAOXAHEXATRIACONTAN-1-OL'>PQE</scene>
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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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|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]
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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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|GENE= glpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])
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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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}}
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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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'''Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae'''
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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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==Overview==
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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 ==
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.
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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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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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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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Haemophilus influenzae]]
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<div class="pdbe-citations 2nr9" style="background-color:#fffaf0;"></div>
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[[Category: Rhomboid protease]]
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[[Category: Single protein]]
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[[Category: Bateman, K S.]]
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[[Category: Cherney, M M.]]
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[[Category: Fischer, S J.]]
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[[Category: James, M N.G.]]
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[[Category: Lemieux, M J.]]
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[[Category: PA6]]
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[[Category: PQE]]
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[[Category: intramembrane peptidase]]
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[[Category: membrane protein]]
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[[Category: rhomboid protease]]
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[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:50:02 2008''
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==See Also==
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*[[Rhomboid protease|Rhomboid protease]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Haemophilus influenzae 86-028NP]]
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[[Category: Large Structures]]
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[[Category: Bateman KS]]
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[[Category: Cherney MM]]
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[[Category: Fischer SJ]]
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[[Category: James MNG]]
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[[Category: Lemieux MJ]]

Current revision

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae

PDB ID 2nr9

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