Sandbox Reserved 1659: Difference between revisions

== Structure==

LntA is a small basic protein of 9.7 kDa. This protein is highly conserved in L. monocytogenes and is absent in almost all non-pathogenic Listeria strains . This characteristic suggests that lntA plays a key role in Listeria’s virulence. The acidic part of LntA is composed of aspartic acid (<scene name='86/868192/Acidic/1'>17,8%</scene>) and the basic part is composed of lysine and arginine (<scene name='86/868192/Basic/1'>18,6%</scene>). LntA folds in a compact helical structure and is composed of 5 alpha-helix, three of them are long antiparallel helix and can be seen as the core of the protein. The two remaining helix stick out the core. The 3 first helix are named <scene name='86/868192/Helix_h1/1'>H1</scene>, <scene name='86/868192/Helix_h2/1'>H2</scene> and <scene name='86/868192/Helix_h3/1'>H3</scene>. The 2 others are <scene name='86/868192/Helix_h4ter/1'>H4</scene> and <scene name='86/868192/Helix_h5/4'>H5</scene>. These residues located in <scene name='86/868192/These_two_helix/1'>these two helixes</scene> display high RMSD values meaning that this region is likely to oscillate. In fact, by studying this protein on pymol we can see it by the thickness and redness of these helixes which means that they have a high RMSD value :

[[Image:pymol1.jpg]]