1y9t: Difference between revisions

Line 1:

[[Image:1y9t.jpg|left|200px]]<br /><applet load="1y9t" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1y9t.jpg|left|200px]]<br /><applet load="1y9t" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1y9t, resolution 1.87Å" />

'''Crystal structure of a type III secretion system protein complexed with the lipid, 1-monohexanoyl-2-hydroxy-sn-glycero-3-phosphate'''<br />

==Overview==

The ability to translocate virulence proteins into host cells through a, type III secretion apparatus (TTSS) is a hallmark of several Gram-negative, pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and, enteropathogenic Escherichia coli. In common with other types of bacterial, secretion apparatus, the assembly of the TTSS complex requires the, preceding formation of its integral outer membrane secretin ring, component. We have determined at 1.5 A the structure of MxiM28-142, the, Shigella pilot protein that is essential for the assembly and membrane, association of the Shigella secretin, MxiD. This represents the first, atomic structure of a secretin pilot protein from the several bacterial, secretion systems containing an orthologous secretin component. A deep, hydrophobic cavity is observed in the novel 'cracked barrel' structure of, MxiM, providing a specific binding domain for the acyl chains of bacterial, lipids, a proposal that is supported by our various lipid/MxiM complex, structures. Isothermal titration analysis shows that the C-terminal domain, of the secretin, MxiD525-570, hinders lipid binding to MxiM.

The ability to translocate virulence proteins into host cells through a type III secretion apparatus (TTSS) is a hallmark of several Gram-negative pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and enteropathogenic Escherichia coli. In common with other types of bacterial secretion apparatus, the assembly of the TTSS complex requires the preceding formation of its integral outer membrane secretin ring component. We have determined at 1.5 A the structure of MxiM28-142, the Shigella pilot protein that is essential for the assembly and membrane association of the Shigella secretin, MxiD. This represents the first atomic structure of a secretin pilot protein from the several bacterial secretion systems containing an orthologous secretin component. A deep hydrophobic cavity is observed in the novel 'cracked barrel' structure of MxiM, providing a specific binding domain for the acyl chains of bacterial lipids, a proposal that is supported by our various lipid/MxiM complex structures. Isothermal titration analysis shows that the C-terminal domain of the secretin, MxiD525-570, hinders lipid binding to MxiM.

==About this Structure==

1Y9T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] with ACT and HHG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Y9T OCA].

1Y9T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=HHG:'>HHG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9T OCA].

==Reference==

Line 13:

[[Category: Shigella flexneri]]

[[Category: Single protein]]

[[Category: Lario, P.I.]]

[[Category: Lario, P I.]]

[[Category: Strynadka, N.C.]]

[[Category: Strynadka, N C.]]

[[Category: ACT]]

[[Category: HHG]]

Line 20:

[[Category: mixed alpha/beta]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 06:38:~~40 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:09 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1y9t.jpg|left|200px]]<br /><applet load="1y9t" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1y9t.jpg|left|200px]]<br /><applet load="1y9t" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1y9t, resolution 1.87&Aring;" />
 '''Crystal structure of a type III secretion system protein complexed with the lipid, 1-monohexanoyl-2-hydroxy-sn-glycero-3-phosphate'''<br />
 ==Overview==
-The ability to translocate virulence proteins into host cells through a, type III secretion apparatus (TTSS) is a hallmark of several Gram-negative, pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and, enteropathogenic Escherichia coli. In common with other types of bacterial, secretion apparatus, the assembly of the TTSS complex requires the, preceding formation of its integral outer membrane secretin ring, component. We have determined at 1.5 A the structure of MxiM28-142, the, Shigella pilot protein that is essential for the assembly and membrane, association of the Shigella secretin, MxiD. This represents the first, atomic structure of a secretin pilot protein from the several bacterial, secretion systems containing an orthologous secretin component. A deep, hydrophobic cavity is observed in the novel 'cracked barrel' structure of, MxiM, providing a specific binding domain for the acyl chains of bacterial, lipids, a proposal that is supported by our various lipid/MxiM complex, structures. Isothermal titration analysis shows that the C-terminal domain, of the secretin, MxiD525-570, hinders lipid binding to MxiM.
+The ability to translocate virulence proteins into host cells through a type III secretion apparatus (TTSS) is a hallmark of several Gram-negative pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and enteropathogenic Escherichia coli. In common with other types of bacterial secretion apparatus, the assembly of the TTSS complex requires the preceding formation of its integral outer membrane secretin ring component. We have determined at 1.5 A the structure of MxiM28-142, the Shigella pilot protein that is essential for the assembly and membrane association of the Shigella secretin, MxiD. This represents the first atomic structure of a secretin pilot protein from the several bacterial secretion systems containing an orthologous secretin component. A deep hydrophobic cavity is observed in the novel 'cracked barrel' structure of MxiM, providing a specific binding domain for the acyl chains of bacterial lipids, a proposal that is supported by our various lipid/MxiM complex structures. Isothermal titration analysis shows that the C-terminal domain of the secretin, MxiD525-570, hinders lipid binding to MxiM.
 ==About this Structure==
-Y9T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] with ACT and HHG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y9T OCA].
+Y9T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=HHG:'>HHG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9T OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Shigella flexneri]]
 [[Category: Single protein]]
-[[Category: Lario, P.I.]]
+[[Category: Lario, P I.]]
-[[Category: Strynadka, N.C.]]
+[[Category: Strynadka, N C.]]
 [[Category: ACT]]
 [[Category: HHG]]
@@ Line 20: / Line 20: @@
 [[Category: mixed alpha/beta]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:38:40 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:09 2008''