Computational study of the outer membrane enzyme Ompla

Image gallery and supplementary information to published work

	      A movie illustrating the active site motion of the
              dimeric enzyme Ompla.

We recently published computational work on OmPLA where we describe molecular dynamics simulations of a monomeric and of two dimeric OmPLA systems embedded in a lipid bilayer. [[Baaden 2003]] The above short movie (58 s, 11 MB) in DivX format illustrates OmPLA active site motions.

	      A graphic depicting the position of the HDS
	      substrate in the membrane inserted Ompla dimer.

The above image shows the position of the HDS substrate in the binding pocket of the OmPLA dimer. Outer and inner leaflet of the bilayer are colored differently, and part of the upper layer as well as all extracellular water are omitted for clarity.

	      A graphic depicting the Ompla dimer interface
	      and the position of the HDS substrate at the

Above, the position of the HDS substrate at the OmPLA monomer-monomer interface is shown in a closeup view (left), the overall monomer-substrate-monomer system is illustrated (center) and the key interactions at the dimer interface are highlighted (right).

	      A collage of several Ompla presentation foils.

A collection of slides about our work on OmPLA can be accessed either online (OmPLA presentation foils), or downloaded as PDF file (OmPLA slides in PDF format).

The main tools used for the preparation of the above materials were VMD, Yasara, MSMS, Tachyon, transcode, iMovie, Raster3D and MagicPoint. © 2003-2005 by Marc Baaden.

[Baaden 2003] M. Baaden, C. Meier and M.S. Sansom : "“A molecular dynamics investigation of mono- and dimeric states of the outer membrane enzyme Ompla”", J.Mol.Biol. 331, 2003, 177-189.

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