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...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2003
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