A Molecular Dynamics Investigation of Mono and Dimeric States of the Outer Membrane Enzyme OMPLA

OMPLA is a phospholipase found in the outer membranes of many Gram-negative bacteria. Enzyme activation requires calcium-induced dimerisation plus bilayer perturbation. As the conformation of OMPLA in the different crystal forms (monomer versus dimer; with/without bound Ca 2+) is remarkably similar...

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Veröffentlicht in:	Journal of molecular biology 2003-08, Vol.331 (1), p.177-189
Hauptverfasser:	Baaden, Marc, Meier, Christoph, Sansom, Mark S.P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Outer Membrane Proteins Bacterial Outer Membrane Proteins - chemistry Binding Sites Ca 2 Calcium Chemical Sciences Computer Simulation Dimerization Enzyme Activation Hydrophobic and Hydrophilic Interactions Lipid Bilayers membrane protein Models, Molecular molecular dynamics OMPLA or physical chemistry Phosphatidylcholines Phospholipases A Phospholipases A - chemistry Phospholipases A1 Protein Conformation substrate-binding cleft Theoretical and
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