1l4i: Difference between revisions

Line 1:

[[Image:1l4i.gif|left|200px]]<br /><applet load="1l4i" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1l4i.gif|left|200px]]<br /><applet load="1l4i" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1l4i, resolution 2.20Å" />

'''Crystal Structure of the Periplasmic Chaperone SfaE'''<br />

==Overview==

S pili are sialic acid binding hair-like appendages expressed by, pathogenic strains of Escherichia coli. The presence of S pili has been, implicated as a virulence factor in both urinary-tract infections and, new-born meningitis. Assembly of S pili proceeds via the ubiquitous, chaperone/usher pathway. Previously, structures of the homologous, chaperones PapD and FimC involved in assembly of P and type-1 pili, respectively, have been solved. Here, the 2.2 A X-ray structure of the S, pilus chaperone SfaE is reported. SfaE has the same overall L-shaped, structure as PapD and FimC, with two immunoglobulin-like domains oriented, at about a 90 degrees angle to each other. Conserved residues in the, subunit-binding cleft known to be critical for chaperone function occupy, essentially identical positions in SfaE, FimC and PapD. As in free PapD, and FimC, the long F1-G1 loop connecting the two last strands of the, N-terminal domain is disordered. SfaE crystallizes as a dimer with an, extensive dimer interface involving the subunit-binding surfaces of the, chaperone. Dimerization via these regions has previously been observed for, PapD and might be a general side effect arising from the subunit-binding, properties of periplasmic chaperones. The domain interface contains an, extended hydrogen-bond network involving three invariant charged residues, and two structurally conserved water molecules. It is suggested that, disruption of the domain interactions may destabilize the N-terminal, domain through exposure of three conserved hydrophobic residues, thereby, promoting release of pilus subunits during pilus assembly.

S pili are sialic acid binding hair-like appendages expressed by pathogenic strains of Escherichia coli. The presence of S pili has been implicated as a virulence factor in both urinary-tract infections and new-born meningitis. Assembly of S pili proceeds via the ubiquitous chaperone/usher pathway. Previously, structures of the homologous chaperones PapD and FimC involved in assembly of P and type-1 pili, respectively, have been solved. Here, the 2.2 A X-ray structure of the S pilus chaperone SfaE is reported. SfaE has the same overall L-shaped structure as PapD and FimC, with two immunoglobulin-like domains oriented at about a 90 degrees angle to each other. Conserved residues in the subunit-binding cleft known to be critical for chaperone function occupy essentially identical positions in SfaE, FimC and PapD. As in free PapD and FimC, the long F1-G1 loop connecting the two last strands of the N-terminal domain is disordered. SfaE crystallizes as a dimer with an extensive dimer interface involving the subunit-binding surfaces of the chaperone. Dimerization via these regions has previously been observed for PapD and might be a general side effect arising from the subunit-binding properties of periplasmic chaperones. The domain interface contains an extended hydrogen-bond network involving three invariant charged residues and two structurally conserved water molecules. It is suggested that disruption of the domain interactions may destabilize the N-terminal domain through exposure of three conserved hydrophobic residues, thereby promoting release of pilus subunits during pilus assembly.

==About this Structure==

1L4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1L4I OCA].

1L4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1L4I OCA].

==Reference==

Line 15:

[[Category: Choudhury, D.]]

[[Category: Hultgren, S.]]

[[Category: Knight, S.D.]]

[[Category: Knight, S D.]]

[[Category: Pinkner, J.]]

[[Category: Stojanoff, V.]]

Line 22:

[[Category: periplasmic chaperone]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:15~~:09 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:15 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1l4i.gif|left|200px]]<br /><applet load="1l4i" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1l4i.gif|left|200px]]<br /><applet load="1l4i" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1l4i, resolution 2.20&Aring;" />
 '''Crystal Structure of the Periplasmic Chaperone SfaE'''<br />
 ==Overview==
-S pili are sialic acid binding hair-like appendages expressed by, pathogenic strains of Escherichia coli. The presence of S pili has been, implicated as a virulence factor in both urinary-tract infections and, new-born meningitis. Assembly of S pili proceeds via the ubiquitous, chaperone/usher pathway. Previously, structures of the homologous, chaperones PapD and FimC involved in assembly of P and type-1 pili, respectively, have been solved. Here, the 2.2 A X-ray structure of the S, pilus chaperone SfaE is reported. SfaE has the same overall L-shaped, structure as PapD and FimC, with two immunoglobulin-like domains oriented, at about a 90 degrees angle to each other. Conserved residues in the, subunit-binding cleft known to be critical for chaperone function occupy, essentially identical positions in SfaE, FimC and PapD. As in free PapD, and FimC, the long F1-G1 loop connecting the two last strands of the, N-terminal domain is disordered. SfaE crystallizes as a dimer with an, extensive dimer interface involving the subunit-binding surfaces of the, chaperone. Dimerization via these regions has previously been observed for, PapD and might be a general side effect arising from the subunit-binding, properties of periplasmic chaperones. The domain interface contains an, extended hydrogen-bond network involving three invariant charged residues, and two structurally conserved water molecules. It is suggested that, disruption of the domain interactions may destabilize the N-terminal, domain through exposure of three conserved hydrophobic residues, thereby, promoting release of pilus subunits during pilus assembly.
+S pili are sialic acid binding hair-like appendages expressed by pathogenic strains of Escherichia coli. The presence of S pili has been implicated as a virulence factor in both urinary-tract infections and new-born meningitis. Assembly of S pili proceeds via the ubiquitous chaperone/usher pathway. Previously, structures of the homologous chaperones PapD and FimC involved in assembly of P and type-1 pili, respectively, have been solved. Here, the 2.2 A X-ray structure of the S pilus chaperone SfaE is reported. SfaE has the same overall L-shaped structure as PapD and FimC, with two immunoglobulin-like domains oriented at about a 90 degrees angle to each other. Conserved residues in the subunit-binding cleft known to be critical for chaperone function occupy essentially identical positions in SfaE, FimC and PapD. As in free PapD and FimC, the long F1-G1 loop connecting the two last strands of the N-terminal domain is disordered. SfaE crystallizes as a dimer with an extensive dimer interface involving the subunit-binding surfaces of the chaperone. Dimerization via these regions has previously been observed for PapD and might be a general side effect arising from the subunit-binding properties of periplasmic chaperones. The domain interface contains an extended hydrogen-bond network involving three invariant charged residues and two structurally conserved water molecules. It is suggested that disruption of the domain interactions may destabilize the N-terminal domain through exposure of three conserved hydrophobic residues, thereby promoting release of pilus subunits during pilus assembly.
 ==About this Structure==
-L4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1L4I OCA].
+L4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1L4I OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Choudhury, D.]]
 [[Category: Hultgren, S.]]
-[[Category: Knight, S.D.]]
+[[Category: Knight, S D.]]
 [[Category: Pinkner, J.]]
 [[Category: Stojanoff, V.]]
@@ Line 22: / Line 22: @@
 [[Category: periplasmic chaperone]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:15:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:15 2008''