2lsv: Difference between revisions

Line 1:

~~'''Unreleased~~ structure~~'''~~

===The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail===

The ~~entry 2lsv~~ is ~~ON HOLD~~ ~~until Paper Publication~~

==Function==

[[http://www.uniprot.org/uniprot/HSP82_YEAST HSP82_YEAST]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.<ref>PMID:17114002</ref>

~~Authors~~: ~~Back, R~~.~~, Dominguez, C~~.~~, Rothe, B~~.~~, Bobo, C., Beaufils, C., Morera, S., Meyer, P., Charpentier, B~~.~~, Branlant, C~~.~~, Allain, F~~.~~, Manival, X~~.

==About this Structure==

[[2lsv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LSV OCA].

~~Description~~: ~~The NMR high resolution structure of yeast Tah1 in complex with the Hsp90~~ C-~~terminal tail~~

==Reference==

[[Category: Saccharomyces cerevisiae s288c]]

[[Category: Allain, F.]]

[[Category: Back, R.]]

[[Category: Beaufils, C.]]

[[Category: Bobo, C.]]

[[Category: Branlant, C.]]

[[Category: Charpentier, B.]]

[[Category: Dominguez, C.]]

[[Category: Manival, X.]]

[[Category: Meyer, P.]]

[[Category: Morera, S.]]

[[Category: Rothe, B.]]

[[Category: Chaperone-binding protein-chaperone complex]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_2lsv|  PDB=2lsv  |  SCENE=  }}
+===The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail===
-The entry 2lsv is ON HOLD  until Paper Publication
+==Function==
+[[http://www.uniprot.org/uniprot/HSP82_YEAST HSP82_YEAST]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.<ref>PMID:17114002</ref>
-Authors: Back, R., Dominguez, C., Rothe, B., Bobo, C., Beaufils, C., Morera, S., Meyer, P., Charpentier, B., Branlant, C., Allain, F., Manival, X.
+==About this Structure==
+[[2lsv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LSV OCA].
-Description: The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail
+==Reference==
+<references group="xtra"/><references/>
+[[Category: Saccharomyces cerevisiae s288c]]
+[[Category: Allain, F.]]
+[[Category: Back, R.]]
+[[Category: Beaufils, C.]]
+[[Category: Bobo, C.]]
+[[Category: Branlant, C.]]
+[[Category: Charpentier, B.]]
+[[Category: Dominguez, C.]]
+[[Category: Manival, X.]]
+[[Category: Meyer, P.]]
+[[Category: Morera, S.]]
+[[Category: Rothe, B.]]
+[[Category: Chaperone-binding protein-chaperone complex]]