7arj: Difference between revisions
New page: '''Unreleased structure''' The entry 7arj is ON HOLD Authors: Description: Category: Unreleased Structures |
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==LolCDE in complex with lipoprotein and AMPPNP complex undimerized form== | |||
<StructureSection load='7arj' size='340' side='right'caption='[[7arj]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7arj]] is a 5 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=7ARJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ARJ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=Z41:[(2S)-2-hexadecanoyloxy-3-oxidanyl-propyl]+hexadecanoate'>Z41</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=7arj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7arj OCA], [https://pdbe.org/7arj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7arj RCSB], [https://www.ebi.ac.uk/pdbsum/7arj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7arj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LOLC_ECOLI LOLC_ECOLI] Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lipoproteins in the outer membrane of Gram-negative bacteria are involved in various vital physiological activities, including multidrug resistance. Synthesized in the cytoplasm and matured in the inner membrane, lipoproteins must be transported to the outer membrane through the Lol pathway mediated by the ATP-binding cassette transporter LolCDE in the inner membrane via an unknown mechanism. Here, we report cryo-EM structures of Escherichia coli LolCDE in apo, lipoprotein-bound, LolA-bound, ADP-bound and AMP-PNP-bound states at a resolution of 3.2-3.8 A, covering the complete lipoprotein transport cycle. Mutagenesis and in vivo viability assays verify features of the structures and reveal functional residues and structural characteristics of LolCDE. The results provide insights into the mechanisms of sorting and transport of outer-membrane lipoproteins and may guide the development of novel therapies against multidrug-resistant Gram-negative bacteria. | |||
Structural basis for bacterial lipoprotein relocation by the transporter LolCDE.,Tang X, Chang S, Zhang K, Luo Q, Zhang Z, Wang T, Qiao W, Wang C, Shen C, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, Dong H Nat Struct Mol Biol. 2021 Apr;28(4):347-355. doi: 10.1038/s41594-021-00573-x. , Epub 2021 Mar 29. PMID:33782615<ref>PMID:33782615</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7arj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ABC transporter 3D structures|ABC transporter 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Chang SH]] | |||
[[Category: Dong CJ]] | |||
[[Category: Dong HH]] | |||
[[Category: Luo QH]] | |||
[[Category: Qiao W]] | |||
[[Category: Tang XD]] | |||
[[Category: Wang C]] | |||
[[Category: Wang T]] | |||
[[Category: Zhang K]] | |||
[[Category: Zhang X]] | |||
[[Category: Zhang ZB]] | |||
[[Category: Zhang ZY]] | |||
[[Category: Zhu XF]] | |||
Latest revision as of 13:51, 23 October 2024
LolCDE in complex with lipoprotein and AMPPNP complex undimerized formLolCDE in complex with lipoprotein and AMPPNP complex undimerized form
Structural highlights
FunctionLOLC_ECOLI Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA. Publication Abstract from PubMedLipoproteins in the outer membrane of Gram-negative bacteria are involved in various vital physiological activities, including multidrug resistance. Synthesized in the cytoplasm and matured in the inner membrane, lipoproteins must be transported to the outer membrane through the Lol pathway mediated by the ATP-binding cassette transporter LolCDE in the inner membrane via an unknown mechanism. Here, we report cryo-EM structures of Escherichia coli LolCDE in apo, lipoprotein-bound, LolA-bound, ADP-bound and AMP-PNP-bound states at a resolution of 3.2-3.8 A, covering the complete lipoprotein transport cycle. Mutagenesis and in vivo viability assays verify features of the structures and reveal functional residues and structural characteristics of LolCDE. The results provide insights into the mechanisms of sorting and transport of outer-membrane lipoproteins and may guide the development of novel therapies against multidrug-resistant Gram-negative bacteria. Structural basis for bacterial lipoprotein relocation by the transporter LolCDE.,Tang X, Chang S, Zhang K, Luo Q, Zhang Z, Wang T, Qiao W, Wang C, Shen C, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, Dong H Nat Struct Mol Biol. 2021 Apr;28(4):347-355. doi: 10.1038/s41594-021-00573-x. , Epub 2021 Mar 29. PMID:33782615[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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