2ca5: Difference between revisions
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[[Image:2ca5.gif|left|200px]]<br /> | [[Image:2ca5.gif|left|200px]]<br /><applet load="2ca5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2ca5" size=" | |||
caption="2ca5, resolution 2.1Å" /> | caption="2ca5, resolution 2.1Å" /> | ||
'''MXIH NEEDLE PROTEIN OF SHIGELLA FLEXNERI (MONOMERIC FORM, RESIDUES 1-78)'''<br /> | '''MXIH NEEDLE PROTEIN OF SHIGELLA FLEXNERI (MONOMERIC FORM, RESIDUES 1-78)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2CA5 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 NA, IPA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. | 2CA5 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=NA:'>NA</scene>, <scene name='pdbligand=IPA:'>IPA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=1:Na+Binding+Site+For+Chain+A'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CA5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: virulence]] | [[Category: virulence]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:33:20 2008'' | ||
Revision as of 11:33, 3 February 2008
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MXIH NEEDLE PROTEIN OF SHIGELLA FLEXNERI (MONOMERIC FORM, RESIDUES 1-78)
OverviewOverview
Type III secretion systems are essential virulence determinants for many, Gram-negative bacterial pathogens. The type III secretion system consists, of cytoplasmic, transmembrane, and extracellular domains. The, extracellular domain is a hollow needle protruding above the bacterial, surface and is held within a basal body that traverses both bacterial, membranes. Effector proteins are translocated, via this external needle, directly into host cells, where they subvert normal cell functions to aid, infection. Physical contact with host cells initiates secretion and leads, to formation of a pore, thought to be contiguous with the needle channel, in the host-cell membrane. Here, we report the crystal structure of the, Shigella flexneri needle subunit MxiH and a complete model for the needle, assembly built into our three-dimensional EM reconstruction. The model, combined with mutagenesis data, reveals that signaling of host-cell, contact is relayed through the needle via intersubunit contacts and, suggests a mode of binding for a tip complex.
About this StructureAbout this Structure
2CA5 is a Single protein structure of sequence from Shigella flexneri with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Molecular model of a type III secretion system needle: Implications for host-cell sensing., Deane JE, Roversi P, Cordes FS, Johnson S, Kenjale R, Daniell S, Booy F, Picking WD, Picking WL, Blocker AJ, Lea SM, Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12529-33. Epub 2006 Aug 3. PMID:16888041
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