1n5b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1n5b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n5b, resolution 2.00&Aring;" /> '''Crystal Structure Of...)
Line 1: Line 1:
-
[[Image:1n5b.gif|left|200px]]<br /><applet load="1n5b" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1n5b.gif|left|200px]]<br /><applet load="1n5b" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n5b, resolution 2.00&Aring;" />
caption="1n5b, resolution 2.00&Aring;" />
'''Crystal Structure Of The Yersinia enterocolitica Molecular Chaperone Syce'''<br />
'''Crystal Structure Of The Yersinia enterocolitica Molecular Chaperone Syce'''<br />
==Overview==
==Overview==
-
The crystal structure of the Yersinia enterocolitica molecular-chaperone, protein SycE, which specifically binds the YopE protein, has been solved, to 2.0 A resolution by molecular replacement. The crystal contains two, SycE dimers per asymmetric unit; a novel feature of this crystal, when, compared with closely related SycE structures, is a well ordered, carboxy-terminal peptide in one protomer of each dimer. The peptide binds, a hydrophobic patch of a neighboring molecule in a manner similar to that, seen in a SycE-YopE chaperone-target complex, suggestive of low-affinity, 'self-binding' through which the carboxy-terminal peptide might suppress, counterproductive interactions with non-target proteins in vivo.
+
The crystal structure of the Yersinia enterocolitica molecular-chaperone protein SycE, which specifically binds the YopE protein, has been solved to 2.0 A resolution by molecular replacement. The crystal contains two SycE dimers per asymmetric unit; a novel feature of this crystal, when compared with closely related SycE structures, is a well ordered carboxy-terminal peptide in one protomer of each dimer. The peptide binds a hydrophobic patch of a neighboring molecule in a manner similar to that seen in a SycE-YopE chaperone-target complex, suggestive of low-affinity 'self-binding' through which the carboxy-terminal peptide might suppress counterproductive interactions with non-target proteins in vivo.
==About this Structure==
==About this Structure==
-
1N5B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. This structure superseeds the now removed PDB entry 1MD1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N5B OCA].
+
1N5B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. This structure supersedes the now removed PDB entry 1MD1. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5B OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yersinia enterocolitica]]
[[Category: Yersinia enterocolitica]]
-
[[Category: McKay, D.B.]]
+
[[Category: McKay, D B.]]
-
[[Category: Trame, C.B.]]
+
[[Category: Trame, C B.]]
[[Category: molecular chaperone]]
[[Category: molecular chaperone]]
[[Category: type iii secretion system]]
[[Category: type iii secretion system]]
[[Category: yersinia enterocolitica]]
[[Category: yersinia enterocolitica]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:58:29 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:27 2008''

Revision as of 12:02, 21 February 2008


1n5b, resolution 2.00Å

Drag the structure with the mouse to rotate

Crystal Structure Of The Yersinia enterocolitica Molecular Chaperone Syce

Overview

The crystal structure of the Yersinia enterocolitica molecular-chaperone protein SycE, which specifically binds the YopE protein, has been solved to 2.0 A resolution by molecular replacement. The crystal contains two SycE dimers per asymmetric unit; a novel feature of this crystal, when compared with closely related SycE structures, is a well ordered carboxy-terminal peptide in one protomer of each dimer. The peptide binds a hydrophobic patch of a neighboring molecule in a manner similar to that seen in a SycE-YopE chaperone-target complex, suggestive of low-affinity 'self-binding' through which the carboxy-terminal peptide might suppress counterproductive interactions with non-target proteins in vivo.

About this Structure

1N5B is a Single protein structure of sequence from Yersinia enterocolitica. This structure supersedes the now removed PDB entry 1MD1. Full crystallographic information is available from OCA.

Reference

Structure of the Yersinia enterocolitica molecular-chaperone protein SycE., Trame CB, McKay DB, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):389-92. Epub 2003, Jan 23. PMID:12554962

Page seeded by OCA on Thu Feb 21 14:02:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools