NalP: Difference between revisions
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<StructureSection load=' | <StructureSection load='1uyn' size='350' side='right' scene='' caption='Translocator domain of autotransporter NALP complex with pentaethylene glycol mpnpdecyl ether and sulfate, [[1uyn]]' pspeed='8'> | ||
The '''Translocator Domain''' for the '''Autotransporter NaIP''' within ''Neisseria meningitidis'' provides a novel protein pore that contains an alpha helix running axially through its hydrophilic center. Classically many outer membrane pores contain a <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/Naip_-_beta_sheet/1'>12-member beta barrel</scene>, which is able to allow for different conditions than the peptidoglycan layer, which would typically stop many types of proteins and ions from passing through. This <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/Alpha_helix/1'>alpha helix </scene> blocks the pore from being totally open and allows for more regulation of what enters and leaves the cell.<ref name="NaIP"> Oomen, Clasien J., Patrick Van Gelder, Peter Van Ulsen, Maya Feijen, Jan Tommassen, and Piet Gros. "Structure of the Translocator Domain of a Bacterial Autotransporter." Www.ncbi.nlm.nih.gov. The EMBO Journal, 11 Mar. 2004. Web. 6 Nov. 2012. <http://www.ncbi.nlm.nih.gov/pmc/articles/PMC381419/>.</ref> | The '''Translocator Domain''' for the '''Autotransporter NaIP''' within ''Neisseria meningitidis'' provides a novel protein pore that contains an alpha helix running axially through its hydrophilic center. Classically many outer membrane pores contain a <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/Naip_-_beta_sheet/1'>12-member beta barrel</scene>, which is able to allow for different conditions than the peptidoglycan layer, which would typically stop many types of proteins and ions from passing through. This <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/Alpha_helix/1'>alpha helix </scene> blocks the pore from being totally open and allows for more regulation of what enters and leaves the cell.<ref name="NaIP"> Oomen, Clasien J., Patrick Van Gelder, Peter Van Ulsen, Maya Feijen, Jan Tommassen, and Piet Gros. "Structure of the Translocator Domain of a Bacterial Autotransporter." Www.ncbi.nlm.nih.gov. The EMBO Journal, 11 Mar. 2004. Web. 6 Nov. 2012. <http://www.ncbi.nlm.nih.gov/pmc/articles/PMC381419/>.</ref> | ||
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==References== | ==References== | ||
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