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| | ==Structure of the soluble domain of Lipooligosaccharide phosphoethanolamine transferase A from Neisseria meningitidis - complex with Zn== | | ==Structure of the soluble domain of Lipooligosaccharide phosphoethanolamine transferase A from Neisseria meningitidis - complex with Zn== |
| - | <StructureSection load='4kay' size='340' side='right' caption='[[4kay]], [[Resolution|resolution]] 1.78Å' scene=''> | + | <StructureSection load='4kay' size='340' side='right'caption='[[4kay]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kay]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimb Neimb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KAY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KAY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kay]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KAY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kay OCA], [https://pdbe.org/4kay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kay RCSB], [https://www.ebi.ac.uk/pdbsum/4kay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kay ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kav|4kav]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB1638 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylglycerophosphatase Phosphatidylglycerophosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.27 3.1.3.27] </span></td></tr>
| + | |
| - | <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=4kay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kay OCA], [http://pdbe.org/4kay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kay RCSB], [http://www.ebi.ac.uk/pdbsum/4kay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kay ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7DD94_NEIMB Q7DD94_NEIMB] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Neimb]] | + | [[Category: Large Structures]] |
| - | [[Category: Phosphatidylglycerophosphatase]] | + | [[Category: Neisseria meningitidis MC58]] |
| - | [[Category: Anandan, A]] | + | [[Category: Anandan A]] |
| - | [[Category: Vrielink, A]] | + | [[Category: Vrielink A]] |
| - | [[Category: Wanty, C]] | + | [[Category: Wanty C]] |
| - | [[Category: Endotoxin biosynthesis]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lpta]]
| + | |
| - | [[Category: Phosphoethanolamine transferase]]
| + | |
| - | [[Category: Phosphotransferase phosphotransferase]]
| + | |
| - | [[Category: Polymyxin resistance]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
Q7DD94_NEIMB
Publication Abstract from PubMed
Gram-negative bacteria, possess an outer membrane envelope consisting of an outer leaflet of lipopolysaccharides (LPS), also called endotoxins, which protect the pathogen from antimicrobial peptides and have multi-faceted roles in virulence. LPS consists of a glycan moiety attached to Lipid A, embedded in the outer membrane. Modification of the lipid A headgroups by phosphoethanolamine or 4-amino-arabinose residues increase resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A phosphoethanolamine transferases are members of the YhjW/YjdB/YijP superfamily and usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane attached to a soluble catalytic domain. In order to understand the catalytic mechanism of lipid A modification by this enzyme the crystal structure of the soluble domain of the protein of the lipid A phosphoethanolamine transferase (LptA) from Neisseria meningitidis has been determined crystallographically and refined to 1.4A resolution. The structure reveals a core hydrolase fold similar to that of alkaline phosphatase. Loop regions in the structure differ, presumably to enable interaction with the membrane localised substrates and to provide substrate specificity. A phosphorylated form of the putative nucleophile, Thr280, is observed. Metal ions present in the active site are coordinated to Thr280 and to residues conserved amongst the family of transferases. The structure reveals the protein components needed for the transferase chemistry however substrate-binding regions are not evident and are likely to reside in the transmembrane domain of the protein.
The structure of the Neisserial Lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin.,Wanty C, Anandan A, Piek S, Walshe J, Ganguly J, Carlson RW, Stubbs KA, Kahler CM, Vrielink A J Mol Biol. 2013 Jun 27. pii: S0022-2836(13)00423-3. doi:, 10.1016/j.jmb.2013.06.029. PMID:23810904[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wanty C, Anandan A, Piek S, Walshe J, Ganguly J, Carlson RW, Stubbs KA, Kahler CM, Vrielink A. The structure of the Neisserial Lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin. J Mol Biol. 2013 Jun 27. pii: S0022-2836(13)00423-3. doi:, 10.1016/j.jmb.2013.06.029. PMID:23810904 doi:10.1016/j.jmb.2013.06.029
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