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| | <StructureSection load='5i5h' size='340' side='right'caption='[[5i5h]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='5i5h' size='340' side='right'caption='[[5i5h]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i5h]] is a 1 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=5I5H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I5H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i5h]] is a 1 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=5I5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I5H FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yejM, yejN, b2188, JW2176 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5i5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i5h OCA], [http://pdbe.org/5i5h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i5h RCSB], [http://www.ebi.ac.uk/pdbsum/5i5h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i5h ProSAT]</span></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=5i5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i5h OCA], [https://pdbe.org/5i5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i5h RCSB], [https://www.ebi.ac.uk/pdbsum/5i5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i5h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/YEJM_ECOLI YEJM_ECOLI] |
| | <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: Dong, C]] | + | [[Category: Dong C]] |
| - | [[Category: Dong, H]] | + | [[Category: Dong H]] |
| - | [[Category: Ecoli 245-586]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
YEJM_ECOLI
Publication Abstract from PubMed
The outer membrane (OM) of Gram-negative bacteria is a unique asymmetric lipid bilayer in which the outer leaflet is composed of lipopolysaccharide (LPS) and the inner leaflet is formed by glycerophospholipid (GPL). The OM plays a fundamental role in protecting Gram-negative bacteria from harsh environments and toxic compounds. The transport and assembly pathways for phospholipids of bacterial OM are unknown. Cardiolipin (CL) plays an important role in OM biogenesis and pathogenesis, and the inner membrane (IM) protein PbgA, containing five transmembrane domains and a globular domain in periplasm has been recently identified as a CL transporter from the IM to the OM with an unknown mechanism. Here we present the first two crystal structures of soluble periplasmic globular domain of PbgA from S. typhimurium and E. coli, which revealed that the globular domains of PbgA resemble the structures of the arylsulfatase protein family and contains a novel core hydrophobic pocket that may be responsible for binding and transporting CLs. Our structural and functional studies shed an important light on the mechanism of CL transport in Gram-negative bacteria from the IM to the OM, which offers great potential for the development of novel antibiotics against multi-drug resistant bacterial infections.
Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteria.,Dong H, Zhang Z, Tang X, Huang S, Li H, Peng B, Dong C Sci Rep. 2016 Aug 4;6:30815. doi: 10.1038/srep30815. PMID:27487745[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dong H, Zhang Z, Tang X, Huang S, Li H, Peng B, Dong C. Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteria. Sci Rep. 2016 Aug 4;6:30815. doi: 10.1038/srep30815. PMID:27487745 doi:http://dx.doi.org/10.1038/srep30815
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