1n0l: Difference between revisions

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[[Image:1n0l.jpg|left|200px]]<br /><applet load="1n0l" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1n0l.jpg|left|200px]]<br /><applet load="1n0l" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1n0l, resolution 2.30Å" />

'''Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli'''<br />

==Overview==

Periplasmic chaperones direct the assembly of adhesive, multi-subunit, pilus fibers that play critical roles in bacterial pathogenesis. Pilus, assembly occurs via a donor strand exchange mechanism in which the, N-terminal extension of one subunit replaces the chaperone G(1) strand, that transiently occupies a groove in the neighboring subunit. Here, we, show that the chaperone primes the subunit for assembly by holding the, groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure, of the groove and seals the N-terminal extension in place. It is this, topological transition, made possible only by the priming action of the, chaperone that drives subunit assembly into the fiber.

Periplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G(1) strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber.

==About this Structure==

1N0L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1N0L OCA].

1N0L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0L OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Protein complex]]

[[Category: Hultgren, S.J.]]

[[Category: Hultgren, S J.]]

[[Category: Pinkner, J.S.]]

[[Category: Pinkner, J S.]]

[[Category: Sauer, F.G.]]

[[Category: Sauer, F G.]]

[[Category: Waksman, G.]]

[[Category: chaperone priming]]

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[[Category: pilus fiber assembly]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 21:51:~~22 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:59 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1n0l.jpg|left|200px]]<br /><applet load="1n0l" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1n0l.jpg|left|200px]]<br /><applet load="1n0l" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1n0l, resolution 2.30&Aring;" />
 '''Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli'''<br />
 ==Overview==
-Periplasmic chaperones direct the assembly of adhesive, multi-subunit, pilus fibers that play critical roles in bacterial pathogenesis. Pilus, assembly occurs via a donor strand exchange mechanism in which the, N-terminal extension of one subunit replaces the chaperone G(1) strand, that transiently occupies a groove in the neighboring subunit. Here, we, show that the chaperone primes the subunit for assembly by holding the, groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure, of the groove and seals the N-terminal extension in place. It is this, topological transition, made possible only by the priming action of the, chaperone that drives subunit assembly into the fiber.
+Periplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G(1) strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber.
 ==About this Structure==
-N0L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N0L OCA].
+N0L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0L OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Protein complex]]
-[[Category: Hultgren, S.J.]]
+[[Category: Hultgren, S J.]]
-[[Category: Pinkner, J.S.]]
+[[Category: Pinkner, J S.]]
-[[Category: Sauer, F.G.]]
+[[Category: Sauer, F G.]]
 [[Category: Waksman, G.]]
 [[Category: chaperone priming]]
@@ Line 23: / Line 23: @@
 [[Category: pilus fiber assembly]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:51:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:59 2008''