6b21: Difference between revisions
New page: '''Unreleased structure''' The entry 6b21 is ON HOLD Authors: Boone, C.D., Laganowsky, A. Description: Crystal structure of AmtB from E. coli bound to TopFluor cardiolipin [[Category: ... |
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==Crystal structure of AmtB from E. coli bound to TopFluor cardiolipin== | |||
<StructureSection load='6b21' size='340' side='right'caption='[[6b21]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6b21]] 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=6B21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B21 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C9V:[(2R,5R,11R,14S,24E)-14-[(acetyloxy)methyl]-8-{[5-(3,5-dimethyl-1H-pyrrol-2-yl-kappaN)-5-(3,5-dimethyl-2H-pyrrol-2-ylidene-kappaN)pentanoyl]oxy}-5,11-dihydroxy-2-{[(9E)-octadec-9-enoyl]oxy}-5,11,16-trioxo-4,6,10,12,15-pentaoxa-5lambda~5~,11lambda~5~-diphosphatritriacont-24-en-1-yl+(9E)-octadec-9-enoatato](difluoro)boron'>C9V</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=6b21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b21 OCA], [https://pdbe.org/6b21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b21 RCSB], [https://www.ebi.ac.uk/pdbsum/6b21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b21 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AMTB_ECOLI AMTB_ECOLI] Involved in the uptake of ammonia. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Membrane proteins interact with a myriad of lipid species in the biological membrane, leading to a bewildering number of possible protein-lipid assemblies. Despite this inherent complexity, the identification of specific protein-lipid interactions and the crucial role of lipids in the folding, structure, and function of membrane proteins is emerging from an increasing number of reports. Fundamental questions remain, however, regarding the ability of specific lipid binding events to membrane proteins to alter remote binding sites for lipids of a different type, a property referred to as allostery [Monod J, Wyman J, Changeux JP (1965) J Mol Biol 12:88-118]. Here, we use native mass spectrometry to determine the allosteric nature of heterogeneous lipid binding events to membrane proteins. We monitored individual lipid binding events to the ammonia channel (AmtB) from Escherichia coli, enabling determination of their equilibrium binding constants. We found that different lipid pairs display a range of allosteric modulation. In particular, the binding of phosphatidylethanolamine and cardiolipin-like molecules to AmtB exhibited the largest degree of allosteric modulation, inspiring us to determine the cocrystal structure of AmtB in this lipid environment. The 2.45-A resolution structure reveals a cardiolipin-like molecule bound to each subunit of the trimeric complex. Mutation of a single residue in AmtB abolishes the positive allosteric modulation observed for binding phosphatidylethanolamine and cardiolipin-like molecules. Our results demonstrate that specific lipid-protein interactions can act as allosteric modulators for the binding of different lipid types to integral membrane proteins. | |||
Allostery revealed within lipid binding events to membrane proteins.,Patrick JW, Boone CD, Liu W, Conover GM, Liu Y, Cong X, Laganowsky A Proc Natl Acad Sci U S A. 2018 Mar 5. pii: 1719813115. doi:, 10.1073/pnas.1719813115. PMID:29507234<ref>PMID:29507234</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Boone | <div class="pdbe-citations 6b21" style="background-color:#fffaf0;"></div> | ||
[[Category: Laganowsky | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Boone CD]] | |||
[[Category: Laganowsky A]] | |||
Latest revision as of 17:30, 4 October 2023
Crystal structure of AmtB from E. coli bound to TopFluor cardiolipinCrystal structure of AmtB from E. coli bound to TopFluor cardiolipin
Structural highlights
FunctionAMTB_ECOLI Involved in the uptake of ammonia. Publication Abstract from PubMedMembrane proteins interact with a myriad of lipid species in the biological membrane, leading to a bewildering number of possible protein-lipid assemblies. Despite this inherent complexity, the identification of specific protein-lipid interactions and the crucial role of lipids in the folding, structure, and function of membrane proteins is emerging from an increasing number of reports. Fundamental questions remain, however, regarding the ability of specific lipid binding events to membrane proteins to alter remote binding sites for lipids of a different type, a property referred to as allostery [Monod J, Wyman J, Changeux JP (1965) J Mol Biol 12:88-118]. Here, we use native mass spectrometry to determine the allosteric nature of heterogeneous lipid binding events to membrane proteins. We monitored individual lipid binding events to the ammonia channel (AmtB) from Escherichia coli, enabling determination of their equilibrium binding constants. We found that different lipid pairs display a range of allosteric modulation. In particular, the binding of phosphatidylethanolamine and cardiolipin-like molecules to AmtB exhibited the largest degree of allosteric modulation, inspiring us to determine the cocrystal structure of AmtB in this lipid environment. The 2.45-A resolution structure reveals a cardiolipin-like molecule bound to each subunit of the trimeric complex. Mutation of a single residue in AmtB abolishes the positive allosteric modulation observed for binding phosphatidylethanolamine and cardiolipin-like molecules. Our results demonstrate that specific lipid-protein interactions can act as allosteric modulators for the binding of different lipid types to integral membrane proteins. Allostery revealed within lipid binding events to membrane proteins.,Patrick JW, Boone CD, Liu W, Conover GM, Liu Y, Cong X, Laganowsky A Proc Natl Acad Sci U S A. 2018 Mar 5. pii: 1719813115. doi:, 10.1073/pnas.1719813115. PMID:29507234[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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