High Resolution Crystallographic Studies Of Alpha-Hemolysin-Phospholipid Complexes Define Heptamer-Lipid Head Group Interactions: Implication For Understanding Protein-Lipid Interactions (370 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2004 Jun; 13(6): 1503-1511.
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Paper type: Journal Article,
Impact factor: 4.116, 5-year impact factor: 3.029
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2442650172&partnerID=40&md5=15257c555a25d7fcf6d689b657507f31
Keywords: Integral Membrane Protein, Pore-Forming Toxin, Protein-Membrane Interactions, Alpha Hemolysin, Ammonium Derivative, Arginine, Bacterial Protein, Dipropanoylglycerophosphocholine, Glycerophosphorylcholine, Lipid, Phospholipid, Pore Protein, Unclassified Drug, Article, Cell Membrane, Channel Gating, Complex Formation, Crystallography, Membrane Binding, Nonhuman, Priority Journal, Protein Binding, Protein Lipid Interaction, Protein Secretion, Solubility, Staphylococcus Aureus, Bacterial Toxins, Crystallization, X-Ray, Hemolysin Proteins, Models, Molecular, Protein Conformation, Sensitivity And Specificity, Bacteria (microorganisms),
Affiliations:
*** IBB - CNR ***
Howard Hughes Medical Institute, Dept. of Biochem./Molec. Biophys., Columbia University, New York, NY 10032, United States
Dipartimento di Chimica Biologica, Ist. di Biostrutture/Bioimmagini-CNR, University of Naples Federico II, 80134, Naples, Italy
References:
Not available.
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2004 Jun; 13(6): 1503-1511.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.116, 5-year impact factor: 3.029
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-2442650172&partnerID=40&md5=15257c555a25d7fcf6d689b657507f31
Keywords: Integral Membrane Protein, Pore-Forming Toxin, Protein-Membrane Interactions, Alpha Hemolysin, Ammonium Derivative, Arginine, Bacterial Protein, Dipropanoylglycerophosphocholine, Glycerophosphorylcholine, Lipid, Phospholipid, Pore Protein, Unclassified Drug, Article, Cell Membrane, Channel Gating, Complex Formation, Crystallography, Membrane Binding, Nonhuman, Priority Journal, Protein Binding, Protein Lipid Interaction, Protein Secretion, Solubility, Staphylococcus Aureus, Bacterial Toxins, Crystallization, X-Ray, Hemolysin Proteins, Models, Molecular, Protein Conformation, Sensitivity And Specificity, Bacteria (microorganisms),
Affiliations:
*** IBB - CNR ***
Howard Hughes Medical Institute, Dept. of Biochem./Molec. Biophys., Columbia University, New York, NY 10032, United States
Dipartimento di Chimica Biologica, Ist. di Biostrutture/Bioimmagini-CNR, University of Naples Federico II, 80134, Naples, Italy
References:
Not available.
High Resolution Crystallographic Studies Of Alpha-Hemolysin-Phospholipid Complexes Define Heptamer-Lipid Head Group Interactions: Implication For Understanding Protein-Lipid Interactions
The α-hemolysin is an archetypal pore-forming protein that is secreted from Staphylococcus aureus as a water-soluble monomer. When the monomer binds to the membrane of a susceptible cell, the membrane-bound molecules assemble into the lytic heptamer. Although a bilayer or a bilayer-like environment are essential to toxin assembly, there is no high resolution information on toxin-phospholipid complexes. We have determined the structures of detergent-solubilized α-hemolysin heptamer bound to glycerophosphocholine or dipropanoyl glycerophosphocholine at 1.75-1.80 Å resolution and 110 K. The phosphocholine head group binds to each subunit in a crevice between the rim and the stem domains. The quaternary ammonium group interacts primarily with aromatic residues, whereas the phosphodiester moiety interacts with a conserved arginine residue. These structures provide a molecular basis for understanding why α-hemolysin preferentially assembles on membranes comprised of phosphocholine lipids.
The α-hemolysin is an archetypal pore-forming protein that is secreted from Staphylococcus aureus as a water-soluble monomer. When the monomer binds to the membrane of a susceptible cell, the membrane-bound molecules assemble into the lytic heptamer. Although a bilayer or a bilayer-like environment are essential to toxin assembly, there is no high resolution information on toxin-phospholipid complexes. We have determined the structures of detergent-solubilized α-hemolysin heptamer bound to glycerophosphocholine or dipropanoyl glycerophosphocholine at 1.75-1.80 Å resolution and 110 K. The phosphocholine head group binds to each subunit in a crevice between the rim and the stem domains. The quaternary ammonium group interacts primarily with aromatic residues, whereas the phosphodiester moiety interacts with a conserved arginine residue. These structures provide a molecular basis for understanding why α-hemolysin preferentially assembles on membranes comprised of phosphocholine lipids.
High Resolution Crystallographic Studies Of Alpha-Hemolysin-Phospholipid Complexes Define Heptamer-Lipid Head Group Interactions: Implication For Understanding Protein-Lipid Interactions
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High Resolution Crystallographic Studies Of Alpha-Hemolysin-Phospholipid Complexes Define Heptamer-Lipid Head Group Interactions: Implication For Understanding Protein-Lipid Interactions
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Cortesi R, Mischiati C, Borgatti M, Breda L, Romanelli A, Saviano M, Pedone C, Gambari R, Nastruzzi C
* Formulations for natural and peptide nucleic acids based on cationic polymeric submicron particles (441 views)
The Aaps Journal (ISSN: 1522-1059, 1550-7416), 2004 Jan 20; 6(1): N/D-N/D.
Impact Factor: 1.938
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* Formulations for natural and peptide nucleic acids based on cationic polymeric submicron particles (441 views)
The Aaps Journal (ISSN: 1522-1059, 1550-7416), 2004 Jan 20; 6(1): N/D-N/D.
Impact Factor: 1.938
View Export to BibTeX Export to EndNote
1 Records (0 excluding Abstracts).
Total impact factor: 1.938 (0 excluding Abstracts).
Total 5 year impact factor: 4.97 (0 excluding Abstracts).
Total impact factor: 1.938 (0 excluding Abstracts).
Total 5 year impact factor: 4.97 (0 excluding Abstracts).
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