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Structural basis of chaperone functi...

Sauer, Frederic George.

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Structural basis of chaperone function and pilus fiber assembly in pathogenic bacteria.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Structural basis of chaperone function and pilus fiber assembly in pathogenic bacteria./
作者:	Sauer, Frederic George.
面頁冊數:	116 p.
附註:	Chair: Scott J. Hultgren.
Contained By:	Dissertation Abstracts International63-10B.
標題:	Biology, Cell. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3068486
ISBN:	0493882294

Structural basis of chaperone function and pilus fiber assembly in pathogenic bacteria.
Sauer, Frederic George.

Structural basis of chaperone function and pilus fiber assembly in pathogenic bacteria. - 116 p.

Chair: Scott J. Hultgren.

Thesis (Ph.D.)--Washington University, 2002.

Adhesive, multi-subunit bacterial pilus fibers play critical roles in pathogenesis. P pili, expressed by uropathogenic <italic>E. coli</italic>, mediate bacterial attachment to glycolipids in the kidney during urinary tract infections. P pili are members of a large family of fibrous organelles assembled by the chaperone-usher pathway. The periplasmic chaperone that directs pilus assembly binds to individual subunits and escorts them to the outer membrane usher, which facilitates subunit polymerization across the outer membrane.

ISBN: 0493882294Subjects--Topical Terms:

1017686
Biology, Cell.

Structural basis of chaperone function and pilus fiber assembly in pathogenic bacteria.
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245 1 0 $a Structural basis of chaperone function and pilus fiber assembly in pathogenic bacteria.
300 $a 116 p.
500 $a Chair: Scott J. Hultgren.
500 $a Source: Dissertation Abstracts International, Volume: 63-10, Section: B, page: 4511.
502 $a Thesis (Ph.D.)--Washington University, 2002.
520 $a Adhesive, multi-subunit bacterial pilus fibers play critical roles in pathogenesis. P pili, expressed by uropathogenic <italic>E. coli</italic>, mediate bacterial attachment to glycolipids in the kidney during urinary tract infections. P pili are members of a large family of fibrous organelles assembled by the chaperone-usher pathway. The periplasmic chaperone that directs pilus assembly binds to individual subunits and escorts them to the outer membrane usher, which facilitates subunit polymerization across the outer membrane.
520 $a Biochemical experiments and the crystal structures of three pilus assembly intermediates presented here reveal the molecular mechanisms of chaperone function and pilus fiber assembly at high-resolution. Each pilus subunit has an immunoglobulin-like (Ig) fold that lacks its C-terminal β-strand, leaving a groove on the subunit surface where this strand would otherwise be. The chaperone, in an interaction termed donor strand complementation, donates its G1 strand to occupy the groove of the subunit and complete its Ig fold. The fold thus produced is atypical, since the G1 strand runs in a parallel orientation in the groove, opposite the canonical direction. Each subunit also has an N-terminal extension that is homologous to the chaperone G1 strand. Pilus assembly proceeds via a donor strand exchange mechanism, in which the N-terminal extension of one subunit displaces the chaperone G1 strand from and occupies the groove of its neighboring subunit in the pilus.
520 $a Donor strand complementation couples the folding of the subunit with the transient capping of its interactive groove and thus prevents non-productive subunit interactions. Simultaneously, donor strand complementation primes the subunit for donor strand exchange. The parallel orientation of the chaperone G1 strand holds the groove in an open, activated conformation. After donor strand exchange the N-terminal extension runs in an anti-parallel, canonical direction and is shifted in register relative to the G1 strand. This reversal of orientation and shift in register allow the groove to close, sealing the N-terminal extension in place. The subunit has now attained its “ground” state in the pilus. The chaperone thus promotes a topological transition in the subunit from an open, non-canonical Ig fold to a closed, canonical fold that ultimately drives pilus fiber assembly.
590 $a School code: 0252.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, Medical. $3 1017681
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710 2 0 $a Washington University. $3 1250147
773 0 $t Dissertation Abstracts International $g 63-10B.
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791 $a Ph.D.
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