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| | <StructureSection load='4p32' size='340' side='right'caption='[[4p32]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='4p32' size='340' side='right'caption='[[4p32]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p32]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P32 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p32]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P32 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p31|4p31]], [[4p33|4p33]]</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=4p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p32 OCA], [https://pdbe.org/4p32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p32 RCSB], [https://www.ebi.ac.uk/pdbsum/4p32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p32 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lptB, yhbG, b3201, JW3168 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p32 OCA], [http://pdbe.org/4p32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p32 RCSB], [http://www.ebi.ac.uk/pdbsum/4p32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p32 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LPTB_ECOLI LPTB_ECOLI]] Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system.<ref>PMID:16765569</ref> <ref>PMID:17056748</ref> <ref>PMID:18424520</ref> | + | [https://www.uniprot.org/uniprot/LPTB_ECOLI LPTB_ECOLI] Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system.<ref>PMID:16765569</ref> <ref>PMID:17056748</ref> <ref>PMID:18424520</ref> |
| | <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kahne, D]] | + | [[Category: Kahne D]] |
| - | [[Category: Lazarus, M B]] | + | [[Category: Lazarus MB]] |
| - | [[Category: Liu, C]] | + | [[Category: Liu C]] |
| - | [[Category: Murphy, L]] | + | [[Category: Murphy L]] |
| - | [[Category: Ruiz, N]] | + | [[Category: Ruiz N]] |
| - | [[Category: Sherman, D J]] | + | [[Category: Sherman DJ]] |
| - | [[Category: Walker, S]] | + | [[Category: Walker S]] |
| - | [[Category: Abc transporter]]
| + | |
| - | [[Category: Atp binding]]
| + | |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nucleotide-binding domain]]
| + | |
| Structural highlights
Function
LPTB_ECOLI Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system.[1] [2] [3]
Publication Abstract from PubMed
The cell surface of Gram-negative bacteria contains lipopolysaccharides (LPS), which provide a barrier against the entry of many antibiotics. LPS assembly involves a multiprotein LPS transport (Lpt) complex that spans from the cytoplasm to the outer membrane. In this complex, an unusual ATP-binding cassette transporter is thought to power the extraction of LPS from the outer leaflet of the cytoplasmic membrane and its transport across the cell envelope. We introduce changes into the nucleotide-binding domain, LptB, that inactivate transporter function in vivo. We characterize these residues using biochemical experiments combined with high-resolution crystal structures of LptB pre- and post-ATP hydrolysis and suggest a role for an active site residue in phosphate exit. We also identify a conserved residue that is not required for ATPase activity but is essential for interaction with the transmembrane components. Our studies establish the essentiality of ATP hydrolysis by LptB to power LPS transport in cells and suggest strategies to inhibit transporter function away from the LptB active site.
Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport.,Sherman DJ, Lazarus MB, Murphy L, Liu C, Walker S, Ruiz N, Kahne D Proc Natl Acad Sci U S A. 2014 Mar 17. PMID:24639492[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sperandeo P, Pozzi C, Deho G, Polissi A. Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus. Res Microbiol. 2006 Jul-Aug;157(6):547-58. Epub 2006 Feb 9. PMID:16765569 doi:10.1016/j.resmic.2005.11.014
- ↑ Sperandeo P, Cescutti R, Villa R, Di Benedetto C, Candia D, Deho G, Polissi A. Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli. J Bacteriol. 2007 Jan;189(1):244-53. Epub 2006 Oct 20. PMID:17056748 doi:http://dx.doi.org/10.1128/JB.01126-06
- ↑ Sperandeo P, Lau FK, Carpentieri A, De Castro C, Molinaro A, Deho G, Silhavy TJ, Polissi A. Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli. J Bacteriol. 2008 Jul;190(13):4460-9. Epub 2008 Apr 18. PMID:18424520 doi:JB.00270-08
- ↑ Sherman DJ, Lazarus MB, Murphy L, Liu C, Walker S, Ruiz N, Kahne D. Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport. Proc Natl Acad Sci U S A. 2014 Mar 17. PMID:24639492 doi:http://dx.doi.org/10.1073/pnas.1323516111
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