2erv: Difference between revisions

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{{Seed}}
[[Image:2erv.png|left|200px]]


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==Crystal structure of the outer membrane enzyme PagL==
The line below this paragraph, containing "STRUCTURE_2erv", creates the "Structure Box" on the page.
<StructureSection load='2erv' size='340' side='right'caption='[[2erv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2erv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERV 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&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CXE:PENTAETHYLENE+GLYCOL+MONODECYL+ETHER'>CXE</scene></td></tr>
{{STRUCTURE_2erv|  PDB=2erv  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2erv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erv OCA], [https://pdbe.org/2erv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2erv RCSB], [https://www.ebi.ac.uk/pdbsum/2erv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2erv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAGL_PSEAE PAGL_PSEAE] Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety. Lacks fatty acyl chain-length specificity as removes both 3-OH C10 and 3-OH C14 fatty acids from lipid A.<ref>PMID:15611102</ref> <ref>PMID:16352835</ref> <ref>PMID:16632613</ref>
== 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/er/2erv_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=2erv ConSurf].
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== Publication Abstract from PubMed ==
Pathogenic gram-negative bacteria can modify the lipid A portion of their lipopolysaccharide in response to environmental stimuli. 3-O-deacylation of lipid A by the outer membrane enzyme PagL modulates signaling through Toll-like receptor 4, leading to a reduced host immune response. We found that PagL is widely disseminated among gram-negative bacteria. Only four residues are conserved: a Ser, His, Phe, and Asn residue. Here, we describe the crystal structure of PagL from Pseudomonas aeruginosa to 2.0-A resolution. It consists of an eight-stranded beta-barrel with the axis tilted by approximately 30 degrees with respect to the lipid bilayer. The structure reveals that PagL contains an active site with a Ser-His-Glu catalytic triad and an oxyanion hole that comprises the conserved Asn. The importance of active site residues was confirmed in mutagenesis studies. Although PagL is most likely active as a monomer, its active site architecture shows high resemblance to that of the dimeric 12-stranded outer membrane phospholipase A. Modeling of the substrate lipid X onto the active site reveals that the 3-O-acyl chain is accommodated in a hydrophobic groove perpendicular to the membrane plane. In addition, an aspartate makes a hydrogen bond with the hydroxyl group of the 3-O-acyl chain, probably providing specificity of PagL toward lipid A.


===Crystal structure of the outer membrane enzyme PagL===
Crystal structure and catalytic mechanism of the LPS 3-O-deacylase PagL from Pseudomonas aeruginosa.,Rutten L, Geurtsen J, Lambert W, Smolenaers JJ, Bonvin AM, de Haan A, van der Ley P, Egmond MR, Gros P, Tommassen J Proc Natl Acad Sci U S A. 2006 May 2;103(18):7071-6. Epub 2006 Apr 21. PMID:16632613<ref>PMID:16632613</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 16632613 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16632613}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2ERV is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERV OCA].
 
==Reference==
<ref group="xtra">PMID:16632613</ref><references group="xtra"/>
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Bonvin, A M.]]
[[Category: Bonvin AM]]
[[Category: Egmond, M R.]]
[[Category: Egmond MR]]
[[Category: Geurtsen, J.]]
[[Category: Geurtsen J]]
[[Category: Gros, P.]]
[[Category: Gros P]]
[[Category: Lambert, W.]]
[[Category: Lambert W]]
[[Category: Ley, P van der.]]
[[Category: Rutten L]]
[[Category: Rutten, L.]]
[[Category: Smolenaers JJ]]
[[Category: Smolenaers, J J.]]
[[Category: Tommassen J]]
[[Category: Tommassen, J.]]
[[Category: Van der Ley P]]
[[Category: Beta barrel]]
[[Category: Enzyme]]
[[Category: Hydrolase]]
[[Category: Lipopolysaccharide]]
[[Category: Membrane protein]]
[[Category: Outer membrane]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:29:57 2009''