2xcu

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==Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP==
==Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP==
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<StructureSection load='2xcu' size='340' side='right' caption='[[2xcu]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
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<StructureSection load='2xcu' size='340' side='right'caption='[[2xcu]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xcu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XCU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XCU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xcu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XCU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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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]] 2.42&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xci|2xci]]</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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xcu OCA], [http://pdbe.org/2xcu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xcu RCSB], [http://www.ebi.ac.uk/pdbsum/2xcu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xcu ProSAT]</span></td></tr>
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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=2xcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xcu OCA], [https://pdbe.org/2xcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xcu RCSB], [https://www.ebi.ac.uk/pdbsum/2xcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xcu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KDTA_AQUAE KDTA_AQUAE]] Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the acceptor lipid.<ref>PMID:19546212</ref>
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[https://www.uniprot.org/uniprot/KDTA_AQUAE KDTA_AQUAE] Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is capable of adding only a single Kdo residue to the acceptor lipid.<ref>PMID:19546212</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 2xcu" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2xcu" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aquifex aeolicus huber and stetter 2001]]
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[[Category: Aquifex aeolicus]]
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[[Category: Hansen, G]]
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[[Category: Large Structures]]
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[[Category: Hilgenfeld, R]]
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[[Category: Hansen G]]
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[[Category: Mamat, U]]
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[[Category: Hilgenfeld R]]
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[[Category: Mesters, J R]]
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[[Category: Mamat U]]
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[[Category: Schmidt, H]]
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[[Category: Mesters JR]]
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[[Category: Glycosyltransferase superfamily b]]
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[[Category: Schmidt H]]
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[[Category: Gsea]]
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[[Category: Gt-b]]
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[[Category: Kdta]]
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[[Category: Transferase]]
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Current revision

Membrane-embedded monofunctional glycosyltransferase WaaA of Aquifex aeolicus, complex with CMP

PDB ID 2xcu

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