7omm: Difference between revisions
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==Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)== | ==Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)== | ||
<StructureSection load='7omm' size='340' side='right'caption='[[7omm]]' scene=''> | <StructureSection load='7omm' size='340' side='right'caption='[[7omm]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OMM FirstGlance]. <br> | <table><tr><td colspan='2'>[[7omm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei], [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OMM FirstGlance]. <br> | ||
</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=7omm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7omm OCA], [https://pdbe.org/7omm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7omm RCSB], [https://www.ebi.ac.uk/pdbsum/7omm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7omm ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=7omm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7omm OCA], [https://pdbe.org/7omm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7omm RCSB], [https://www.ebi.ac.uk/pdbsum/7omm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7omm ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/LPTD_NEIG1 LPTD_NEIG1] Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.[HAMAP-Rule:MF_01411] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram-negative bacteria. The last step of LPS insertion via the Lpt pathway is mediated by the LptD/E protein complex. Detailed insights into the architecture of LptDE transporter complexes have been derived from X-ray crystallography. However, no structure of a laterally open LptD transporter, a transient state that occurs during LPS release, is available to date. Here, we report a cryo-EM structure of a partially opened LptDE transporter in complex with rigid chaperones derived from nanobodies, at 3.4 A resolution. In addition, a subset of particles allows to model a structure of a laterally fully opened LptDE complex. Our work offers insights into the mechanism of LPS insertion, provides a structural framework for the development of antibiotics targeting LptD and describes a highly rigid chaperone scaffold to enable structural biology of challenging protein targets. | |||
Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation.,Botte M, Ni D, Schenck S, Zimmermann I, Chami M, Bocquet N, Egloff P, Bucher D, Trabuco M, Cheng RKY, Brunner JD, Seeger MA, Stahlberg H, Hennig M Nat Commun. 2022 Apr 5;13(1):1826. doi: 10.1038/s41467-022-29459-2. PMID:35383177<ref>PMID:35383177</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7omm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Methanosarcina mazei]] | |||
[[Category: Neisseria gonorrhoeae]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Bocquet N]] | [[Category: Bocquet N]] | ||
[[Category: Botte M]] | [[Category: Botte M]] | ||
Latest revision as of 14:17, 23 October 2024
Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)
Structural highlights
FunctionLPTD_NEIG1 Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.[HAMAP-Rule:MF_01411] Publication Abstract from PubMedLipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram-negative bacteria. The last step of LPS insertion via the Lpt pathway is mediated by the LptD/E protein complex. Detailed insights into the architecture of LptDE transporter complexes have been derived from X-ray crystallography. However, no structure of a laterally open LptD transporter, a transient state that occurs during LPS release, is available to date. Here, we report a cryo-EM structure of a partially opened LptDE transporter in complex with rigid chaperones derived from nanobodies, at 3.4 A resolution. In addition, a subset of particles allows to model a structure of a laterally fully opened LptDE complex. Our work offers insights into the mechanism of LPS insertion, provides a structural framework for the development of antibiotics targeting LptD and describes a highly rigid chaperone scaffold to enable structural biology of challenging protein targets. Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation.,Botte M, Ni D, Schenck S, Zimmermann I, Chami M, Bocquet N, Egloff P, Bucher D, Trabuco M, Cheng RKY, Brunner JD, Seeger MA, Stahlberg H, Hennig M Nat Commun. 2022 Apr 5;13(1):1826. doi: 10.1038/s41467-022-29459-2. PMID:35383177[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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