2co3: Difference between revisions
New page: left|200px<br /><applet load="2co3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2co3, resolution 1.78Å" /> '''SALMONELLA ENTERICA ... |
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==Overview== | ==Overview== | ||
Gram-negative pathogens commonly use the chaperone-usher pathway to | Gram-negative pathogens commonly use the chaperone-usher pathway to assemble adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a chaperone that donates a beta strand to complement the subunits' truncated immunoglobulin-like fold. Pilus assembly proceeds through a "donor-strand exchange" (DSE) mechanism whereby this complementary beta strand is replaced by the N-terminal extension (Nte) of an incoming pilus subunit. Using X-ray crystallography and real-time electrospray ionization mass spectrometry (ESI-MS), we demonstrate that DSE requires the formation of a transient ternary complex between the chaperone-subunit complex and the Nte of the next subunit to be assembled. The process is crucially dependent on an initiation site (the P5 pocket) needed to recruit the incoming Nte. The data also suggest a capping reaction displacing DSE toward product formation. These results support a zip-in-zip-out mechanism for DSE and a catalytic role for the usher, the molecular platform at which pili are assembled. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ashcroft, A | [[Category: Ashcroft, A E.]] | ||
[[Category: Hannan, T | [[Category: Hannan, T J.]] | ||
[[Category: Hultgren, S | [[Category: Hultgren, S J.]] | ||
[[Category: Radford, S | [[Category: Radford, S E.]] | ||
[[Category: Remaut, H.]] | [[Category: Remaut, H.]] | ||
[[Category: Rose, R | [[Category: Rose, R J.]] | ||
[[Category: Waksman, G.]] | [[Category: Waksman, G.]] | ||
[[Category: adhesion]] | [[Category: adhesion]] | ||
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[[Category: pilus subunit]] | [[Category: pilus subunit]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:50:41 2008'' | ||
Revision as of 17:50, 21 February 2008
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SALMONELLA ENTERICA SAFA PILIN, HEAD-TO-TAIL SWAPPED DIMER OF NTD1 MUTANT
OverviewOverview
Gram-negative pathogens commonly use the chaperone-usher pathway to assemble adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a chaperone that donates a beta strand to complement the subunits' truncated immunoglobulin-like fold. Pilus assembly proceeds through a "donor-strand exchange" (DSE) mechanism whereby this complementary beta strand is replaced by the N-terminal extension (Nte) of an incoming pilus subunit. Using X-ray crystallography and real-time electrospray ionization mass spectrometry (ESI-MS), we demonstrate that DSE requires the formation of a transient ternary complex between the chaperone-subunit complex and the Nte of the next subunit to be assembled. The process is crucially dependent on an initiation site (the P5 pocket) needed to recruit the incoming Nte. The data also suggest a capping reaction displacing DSE toward product formation. These results support a zip-in-zip-out mechanism for DSE and a catalytic role for the usher, the molecular platform at which pili are assembled.
About this StructureAbout this Structure
2CO3 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
ReferenceReference
Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism., Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G, Mol Cell. 2006 Jun 23;22(6):831-42. PMID:16793551
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