1g41: Difference between revisions

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[[Image:1g41.~~jpg~~|left|200px]]

[[Image:1g41.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE~~'''~~

===CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE===

~~==Overview==~~

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The ~~structure of the Haemophilus influenzae HslU protein~~, ~~a molecular chaperone of the Clp/Hsp100 family~~, ~~has been solved to 2.3 A by molecular replacement using a model of the homologous Escherichia coli protein. The crystals in which~~ the ~~structure was solved have an unusual twinning, or one-dimensional disorder, in which each successive crystal-packing layer is displaced laterally relative~~ to the ~~one below~~ it. ~~A model for the twinning and an algorithm for detwinning the data are described~~. It is ~~known from other work that when~~ the ~~HslU hexamer binds its cognate protease HslV, the carboxy-terminal helices of HslU protomers distend and bind between HslV subunits~~. ~~Comparison of HslU alone with its structure in the HslUV complex reveals several conserved amino~~-~~acid residues whose side~~-~~chain interactions differ between the two structures, suggesting that they may be part of a conformational switch that facilitates the release of the HslU carboxy-terminal helices when HslV binds.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11468391}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11468391 is the PubMed ID number.

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==About this Structure==

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[[Category: Atp-dependent proteolysis]]

[[Category: Clpy]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 17~~:06:39 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:22:52 2008''

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-[[Image:1g41.jpg|left|200px]]
+{{Seed}}
+[[Image:1g41.png|left|200px]]
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 {{STRUCTURE_1g41|  PDB=1g41  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE'''
+===CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE===
-==Overview==
+<!--
-The structure of the Haemophilus influenzae HslU protein, a molecular chaperone of the Clp/Hsp100 family, has been solved to 2.3 A by molecular replacement using a model of the homologous Escherichia coli protein. The crystals in which the structure was solved have an unusual twinning, or one-dimensional disorder, in which each successive crystal-packing layer is displaced laterally relative to the one below it. A model for the twinning and an algorithm for detwinning the data are described. It is known from other work that when the HslU hexamer binds its cognate protease HslV, the carboxy-terminal helices of HslU protomers distend and bind between HslV subunits. Comparison of HslU alone with its structure in the HslUV complex reveals several conserved amino-acid residues whose side-chain interactions differ between the two structures, suggesting that they may be part of a conformational switch that facilitates the release of the HslU carboxy-terminal helices when HslV binds.
+The line below this paragraph, {{ABSTRACT_PUBMED_11468391}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11468391 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11468391}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Atp-dependent proteolysis]]
 [[Category: Clpy]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:06:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:22:52 2008''