1n5b: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1n5b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n5b, resolution 2.00Å" /> '''Crystal Structure Of...
 
OCA (talk | contribs)
No edit summary
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''