2co7
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 ... | + | 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== | ||
| - | 2CO7 is a | + | 2CO7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CO7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: strand complementation]] | [[Category: strand complementation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:44:33 2007'' |
Revision as of 10:39, 5 November 2007
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SALMONELLA ENTERICA SAFA PILIN IN COMPLEX WITH THE SAFB CHAPERONE (TYPE II)
Overview
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
2CO7 is a Protein complex structure of sequences from Salmonella typhimurium with SO4 as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 5 12:44:33 2007
