NalP: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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

Revision as of 13:11, 16 August 2017 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary ← Older edit		Revision as of 13:50, 16 August 2017 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary Newer edit →
Line 1:		Line 1:
	<StructureSection load='1UYN' size='350' side='right' scene='' caption='Translocator domain of autotransporter NALP complex with pentaethylene glycol mpnpdecyl ether and sulfate, [[1uyn]]'>		<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>