2nr9

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==Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae==
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[[Image:2nr9.png|left|200px]]
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<StructureSection load='2nr9' size='340' side='right' caption='[[2nr9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2nr9]] is a 1 chain structure with 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]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ic8|2ic8]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2nr9 RCSB], [http://www.ebi.ac.uk/pdbsum/2nr9 PDBsum]</span></td></tr>
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<table>
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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/chain_selection.php?pdb_ID=2ata 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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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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The line below this paragraph, containing "STRUCTURE_2nr9", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2nr9| PDB=2nr9 | SCENE= }}
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===Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<!--
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_17210913}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 17210913 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_17210913}}
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==About this Structure==
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2NR9 is a 1 chain 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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<ref group="xtra">PMID:17210913</ref><references group="xtra"/>
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Rhomboid protease]]
[[Category: Rhomboid protease]]
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Rhomboid protease]]
[[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 Tue Feb 17 06:23:34 2009''
 

Revision as of 08:39, 7 May 2014

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae

2nr9, resolution 2.20Å

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