2iua

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{{Seed}}
 
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[[Image:2iua.png|left|200px]]
 
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==C. trachomatis LpxD==
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The line below this paragraph, containing "STRUCTURE_2iua", creates the "Structure Box" on the page.
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<StructureSection load='2iua' size='340' side='right'caption='[[2iua]], [[Resolution|resolution]] 2.70&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'>[[2iua]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.7&#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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2iua| PDB=2iua | 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=2iua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iua OCA], [https://pdbe.org/2iua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iua RCSB], [https://www.ebi.ac.uk/pdbsum/2iua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iua ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LPXD_CHLTR LPXD_CHLTR] Catalyzes the N-acylation of UDP-3-O-myristoylglucosamine using 3-hydroxyarachidoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (Probable).<ref>PMID:10358025</ref>
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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/iu/2iua_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=2iua 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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The external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable LPS. The biosynthesis of LPS relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine in Chlamydia trachomatis. Our crystallographic study reveals that LpxD is a homotrimer, each subunit of which is constructed from a novel combination of an N-terminal uridine-binding domain, a core lipid-binding domain, and a C-terminal helical extension. Highly conserved residues dominate nucleotide binding. Phe-43 and Tyr-49 form pi-stacking interactions with uracil, and Asn-46 and His-284 form hydrogen bonds with the phosphate groups. These interactions place the glucosamine moiety at the catalytic center formed by two adjacent subunits. Here His-247 and His-284 contribute to a mechanism involving nucleophilic attack by the amine of one substrate on the carbonyl carbon of an acyl carrier protein thioester conjugate. Serendipitously, our study reveals a fatty acid (FA) binding groove near the catalytic center. MS elucidated the presence of a FA mixture binding to LpxD, with palmitic acid the most prevalent. The placement of UDP-N-acetylglucosamine and the FA provides details of N-acyltransferase ligand interactions and allows for a description of structure and reactivity at an early stage of LPS assembly.
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===C. TRACHOMATIS LPXD===
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Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.,Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4321-6. Epub 2007 Mar 5. PMID:17360522<ref>PMID:17360522</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2iua" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17360522}}, adds the Publication Abstract to the page
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*[[UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase|UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17360522 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17360522}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2IUA is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUA OCA].
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==Reference==
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<ref group="xtra">PMID:17360522</ref><references group="xtra"/>
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[[Category: Chlamydia trachomatis]]
[[Category: Chlamydia trachomatis]]
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[[Category: Buetow, L.]]
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[[Category: Large Structures]]
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[[Category: Dawson, A.]]
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[[Category: Buetow L]]
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[[Category: Fyffe, S.]]
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[[Category: Dawson A]]
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[[Category: Hunter, W N.]]
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[[Category: Fyffe S]]
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[[Category: Smith, T K.]]
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[[Category: Hunter WN]]
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[[Category: Acyltransferase]]
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[[Category: Smith TK]]
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[[Category: Enzyme]]
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[[Category: Homotrimer]]
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[[Category: Left-handed beta helix]]
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[[Category: Lipid a biosynthesis]]
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[[Category: Lipid synthesis]]
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[[Category: Transferase]]
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[[Category: Udp-3- o-acyl-glucosamine n-acyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 22 10:44:44 2009''
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Current revision

C. trachomatis LpxD

PDB ID 2iua

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