NalP: Difference between revisions
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< | <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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Recent research has showed that there are possible conserved features to this pore and pores in other types of gram-negative bacteria. Autotransporters that also have the conserved structure of an alpha helix directly preceding the beta core include: AidaI of E. coli, BrkA of B. pertussis, Hap of Hemophilus influenzae and IgA protease and App of N. meningitidis. Much of the these proteins show low conservation within their alpha helixes yet they all have a long traversing alpha helix that leads into the 12 sheeted beta barrel. Due to the amount of research being done on the Neisseria meningitidis' NalPβ protein, its crystal structure is being used in order to model autotransporter secretion. <ref name="NaIP" /> | Recent research has showed that there are possible conserved features to this pore and pores in other types of gram-negative bacteria. Autotransporters that also have the conserved structure of an alpha helix directly preceding the beta core include: AidaI of E. coli, BrkA of B. pertussis, Hap of Hemophilus influenzae and IgA protease and App of N. meningitidis. Much of the these proteins show low conservation within their alpha helixes yet they all have a long traversing alpha helix that leads into the 12 sheeted beta barrel. Due to the amount of research being done on the Neisseria meningitidis' NalPβ protein, its crystal structure is being used in order to model autotransporter secretion. <ref name="NaIP" /> | ||
</StructureSection> | |||
== 3D structure of NalP == | |||
[[1uyn]], [[1uyo]] - NalP - ''Neisseria meningitides'' <br /> | |||
==References== | ==References== | ||
<references /> | <references /> | ||
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