NalP - Revision history

Michal Harel at 17:57, 20 October 2017

2017-10-20T17:57:50Z

←Older revision		Revision as of 17:57, 20 October 2017
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	==References==		==References==
	<references />		<references />
		+	[[Category:Topic Page]]

Joel L. Sussman at 20:52, 16 August 2017

2017-08-16T20:52:58Z

←Older revision		Revision as of 20:52, 16 August 2017
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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'>	+	<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>

Alexander Berchansky at 10:50, 16 August 2017

2017-08-16T10:50:50Z

←Older revision		Revision as of 10:50, 16 August 2017
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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]]'>	+	<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>

Alexander Berchansky at 10:11, 16 August 2017

2017-08-16T10:11:58Z

←Older revision		Revision as of 10:11, 16 August 2017
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-	<~~Structure~~ load='1UYN' size='350' ~~frame~~='~~true~~' ~~align~~='~~right~~' caption='Translocator domain of autotransporter NALP complex with pentaethylene glycol mpnpdecyl ether and sulfate, [[1uyn]]' ~~scene='Insert optional scene name here' /~~>	+	<StructureSection load='1UYN' size='350' side='right' scene='' caption='Translocator domain of autotransporter NALP complex with pentaethylene glycol mpnpdecyl ether and sulfate, [[1uyn]]'>
		+
	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 ==		== 3D structure of NalP ==

Jaime Prilusky: Translocator Domain of the Autotransporter NalP within Neisseria meningitidis moved to NalP: requested by Editor

2016-02-25T12:19:21Z

Translocator Domain of the Autotransporter NalP within Neisseria meningitidis moved to NalP: requested by Editor

←Older revision

Revision as of 12:19, 25 February 2016

Michal Harel at 11:33, 25 February 2016

2016-02-25T11:33:39Z

←Older revision		Revision as of 11:33, 25 February 2016
Line 59:		Line 59:
	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" />

		+	== 3D structure of NalP ==

		+	[[1uyn]], [[1uyo]] - NalP - ''Neisseria meningitides'' <br />
	==References==		==References==
	<references />		<references />

Michal Harel at 11:29, 25 February 2016

2016-02-25T11:29:09Z

←Older revision		Revision as of 11:29, 25 February 2016
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	<Structure load='1UYN' size='350' frame='true' align='right' caption='Translocator domain of autotransporter NALP complex with pentaethylene glycol mpnpdecyl ether and sulfate, [[1uyn]]' scene='Insert optional scene name here' />		<Structure load='1UYN' size='350' frame='true' align='right' caption='Translocator domain of autotransporter NALP complex with pentaethylene glycol mpnpdecyl ether and sulfate, [[1uyn]]' scene='Insert optional scene name here' />
-	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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Michal Harel at 10:44, 14 July 2013

2013-07-14T10:44:41Z

←Older revision		Revision as of 10:44, 14 July 2013
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-	== Neisseria meningitides ==	+	== ''Neisseria meningitides'' ==

-	Neisseria meningitides is a bacterium that infects humans and is the leading cause of “Meningitis (inflammation of the membranes surrounding the brain and spinal cord) is a common form of meningococcal disease and is characterized by fever, severe headache, and stiff neck. Patients with meningococcal sepsis (severe illness caused by bacteria or their toxins in the blood) may present with high fever, hypotension (low blood pressure), and profound weakness. In either case, patients may develop a characteristic rash including petechiae (pinpoint red spots that do not blanch with pressure) or purpura (purple areas similar to bruises) that are caused by bleeding into the skin. Purpura fulminans (hemorrhagic condition resulting in tissue necrosis and small vessel thrombosis) can result in scarring or limb amputations. Approximately 10-14% of cases of meningococcal disease are fatal. Of patients who recover, 11-19% have permanent hearing loss, mental retardation, loss of limbs or other severe sequelae." <ref>"Neisseria Meningitidis." Neisseria Meningitidis. Georgia Department of Public Health, n.d. Web. 13 Nov. 2012. <http://health.state.ga.us/epi/bacterial/path-neisseria.asp>.</ref> For this reason major amounts of research is being done on this bacteria and its transport mechanisms.	+	''Neisseria meningitides'' is a bacterium that infects humans and is the leading cause of “Meningitis (inflammation of the membranes surrounding the brain and spinal cord) is a common form of meningococcal disease and is characterized by fever, severe headache, and stiff neck. Patients with meningococcal sepsis (severe illness caused by bacteria or their toxins in the blood) may present with high fever, hypotension (low blood pressure), and profound weakness. In either case, patients may develop a characteristic rash including petechiae (pinpoint red spots that do not blanch with pressure) or purpura (purple areas similar to bruises) that are caused by bleeding into the skin. Purpura fulminans (hemorrhagic condition resulting in tissue necrosis and small vessel thrombosis) can result in scarring or limb amputations. Approximately 10-14% of cases of meningococcal disease are fatal. Of patients who recover, 11-19% have permanent hearing loss, mental retardation, loss of limbs or other severe sequelae." <ref>"Neisseria Meningitidis." Neisseria Meningitidis. Georgia Department of Public Health, n.d. Web. 13 Nov. 2012. <http://health.state.ga.us/epi/bacterial/path-neisseria.asp>.</ref> For this reason major amounts of research is being done on this bacteria and its transport mechanisms.

	==Structure==		==Structure==

Michal Harel at 10:44, 14 July 2013

2013-07-14T10:44:12Z

←Older revision		Revision as of 10:44, 14 July 2013
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-	<Structure load='1UYN' size='350' frame='true' align='right' caption='Translocator domain of autotransporter NALP, [[1uyn]]' scene='Insert optional scene name here' />	+	<Structure load='1UYN' size='350' frame='true' align='right' caption='Translocator domain of autotransporter NALP complex with pentaethylene glycol mpnpdecyl ether and sulfate, [[1uyn]]' scene='Insert optional scene name here' />
	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>

Michal Harel at 11:42, 17 March 2013

2013-03-17T11:42:11Z

←Older revision		Revision as of 11:42, 17 March 2013
Line 1:		Line 1:
	<Structure load='1UYN' size='350' frame='true' align='right' caption='Translocator domain of autotransporter NALP, [[1uyn]]' scene='Insert optional scene name here' />		<Structure load='1UYN' size='350' frame='true' align='right' caption='Translocator domain of autotransporter NALP, [[1uyn]]' scene='Insert optional scene name here' />
-	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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