1yj7
From Proteopedia
(New page: 200px<br /><applet load="1yj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yj7, resolution 1.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:1yj7.gif|left|200px]]<br /><applet load="1yj7" size=" | + | [[Image:1yj7.gif|left|200px]]<br /><applet load="1yj7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yj7, resolution 1.8Å" /> | caption="1yj7, resolution 1.8Å" /> | ||
'''Crystal structure of enteropathogenic E.coli (EPEC) type III secretion system protein EscJ'''<br /> | '''Crystal structure of enteropathogenic E.coli (EPEC) type III secretion system protein EscJ'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Type III secretion systems (TTSSs) are multi-protein macromolecular | + | Type III secretion systems (TTSSs) are multi-protein macromolecular 'machines' that have a central function in the virulence of many Gram-negative pathogens by directly mediating the secretion and translocation of bacterial proteins (termed effectors) into the cytoplasm of eukaryotic cells. Most of the 20 unique structural components constituting this secretion apparatus are highly conserved among animal and plant pathogens and are also evolutionarily related to proteins in the flagellar-specific export system. Recent electron microscopy experiments have revealed the gross 'needle-shaped' morphology of the TTSS, yet a detailed understanding of the structural characteristics and organization of these protein components within the bacterial membranes is lacking. Here we report the 1.8-A crystal structure of EscJ from enteropathogenic Escherichia coli (EPEC), a member of the YscJ/PrgK family whose oligomerization represents one of the earliest events in TTSS assembly. Crystal packing analysis and molecular modelling indicate that EscJ could form a large 24-subunit 'ring' superstructure with extensive grooves, ridges and electrostatic features. Electron microscopy, labelling and mass spectrometry studies on the orthologous Salmonella typhimurium PrgK within the context of the assembled TTSS support the stoichiometry, membrane association and surface accessibility of the modelled ring. We propose that the YscJ/PrgK protein family functions as an essential molecular platform for TTSS assembly. |
==About this Structure== | ==About this Structure== | ||
| - | 1YJ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YJ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJ7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Felise, H | + | [[Category: Felise, H B.]] |
| - | [[Category: Finlay, B | + | [[Category: Finlay, B B.]] |
| - | [[Category: Frey, E | + | [[Category: Frey, E A.]] |
| - | [[Category: Kimbrough, T | + | [[Category: Kimbrough, T G.]] |
| - | [[Category: Miller, S | + | [[Category: Miller, S I.]] |
| - | [[Category: Pfuetzner, R | + | [[Category: Pfuetzner, R A.]] |
| - | [[Category: Strynadka, N | + | [[Category: Strynadka, N C.J.]] |
| - | [[Category: Thomas, N | + | [[Category: Thomas, N A.]] |
[[Category: Vuckovic, M.]] | [[Category: Vuckovic, M.]] | ||
| - | [[Category: Yip, C | + | [[Category: Yip, C K.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
| Line 28: | Line 28: | ||
[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:51 2008'' |
Revision as of 14:05, 21 February 2008
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Crystal structure of enteropathogenic E.coli (EPEC) type III secretion system protein EscJ
Overview
Type III secretion systems (TTSSs) are multi-protein macromolecular 'machines' that have a central function in the virulence of many Gram-negative pathogens by directly mediating the secretion and translocation of bacterial proteins (termed effectors) into the cytoplasm of eukaryotic cells. Most of the 20 unique structural components constituting this secretion apparatus are highly conserved among animal and plant pathogens and are also evolutionarily related to proteins in the flagellar-specific export system. Recent electron microscopy experiments have revealed the gross 'needle-shaped' morphology of the TTSS, yet a detailed understanding of the structural characteristics and organization of these protein components within the bacterial membranes is lacking. Here we report the 1.8-A crystal structure of EscJ from enteropathogenic Escherichia coli (EPEC), a member of the YscJ/PrgK family whose oligomerization represents one of the earliest events in TTSS assembly. Crystal packing analysis and molecular modelling indicate that EscJ could form a large 24-subunit 'ring' superstructure with extensive grooves, ridges and electrostatic features. Electron microscopy, labelling and mass spectrometry studies on the orthologous Salmonella typhimurium PrgK within the context of the assembled TTSS support the stoichiometry, membrane association and surface accessibility of the modelled ring. We propose that the YscJ/PrgK protein family functions as an essential molecular platform for TTSS assembly.
About this Structure
1YJ7 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural characterization of the molecular platform for type III secretion system assembly., Yip CK, Kimbrough TG, Felise HB, Vuckovic M, Thomas NA, Pfuetzner RA, Frey EA, Finlay BB, Miller SI, Strynadka NC, Nature. 2005 Jun 2;435(7042):702-7. PMID:15931226
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