NalP: Difference between revisions

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Chris Casey, Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman

Revision as of 02:40, 14 November 2012 view source Chris Casey (talk \| contribs) 34 edits No edit summary ← Older edit		Revision as of 02:46, 14 November 2012 view source Chris Casey (talk \| contribs) 34 edits No edit summary Newer edit →
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	===Beta Barrel===		===Beta Barrel===

	The beta barrel is a unique structure that makes this pore is able to allow for transportation in and out of the gram-negative cell. This beta barrel is created with 12 anti-parallel beta-pleated sheets that have wrapped around creating anti-parellel interaction between sheet one and sheet 12. This creates a tube structure that transcends through the membrane of a cell creating a new environment that allows for polar molecules to move through the cell membrane and cell wall when they would have otherwise been stopped by the hydrophobic center of peptidoglycan. The start and end of the beta barrel is on the periplasmic side of the membrane and a short tight turn, <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/T0/1'>T0</scene>, connects the alpha helix to the N-terminal beta strand. The alpha helix has its N-terminus side facing outward toward extracellular material. <ref name="PMID: 8254661"> PMID: 8254661 </ref>		The beta barrel is a unique structure that makes this pore able to allow for transportation in and out of the gram-negative cell. This beta barrel is created with 12 anti-parallel beta-pleated sheets that have wrapped around creating anti-parellel interaction between sheet one and sheet 12. This creates a tube structure that transcends through the membrane of a cell creating a new environment that allows for polar molecules to move through the cell membrane and cell wall when they would have otherwise been stopped by the hydrophobic center of peptidoglycan. The start and end of the beta barrel is on the periplasmic side of the membrane and a short tight turn, <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/T0/1'>T0</scene>, connects the alpha helix to the N-terminal beta strand. The alpha helix has its N-terminus side facing outward toward extracellular material. <ref name="PMID: 8254661"> PMID: 8254661 </ref>