2yey: Difference between revisions
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==Crystal structure of the allosteric-defective chaperonin GroEL E434K mutant== | |||
<StructureSection load='2yey' size='340' side='right' caption='[[2yey]], [[Resolution|resolution]] 4.50Å' scene=''> | |||
=== | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yey]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fbh 3fbh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YEY FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yey OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yey RCSB], [http://www.ebi.ac.uk/pdbsum/2yey PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. The simultaneous positive intra-ring and negative inter-ring co-operativities alternate the functionality of the folding cavities in both protein rings. Negative inter-ring co-operativity is maintained through different inter-ring interactions, including a salt bridge involving Glu 461. Replacement of this residue by Lys modifies the temperature sensitivity of the substrate-folding activity of this protein, most likely as a result of the loss of inter-ring co-operativity. The crystal structure of the mutant chaperonin GroELE461K has been determined at 3.3A and compared with other structures: the wild-type GroEL, an allosteric defective GroEL double mutant and the GroEL-GroES-(ADP)7 complex. The inter-ring region of the mutant exhibits the following characteristics: (i) no salt-bridge stabilizes the inter-ring interface; (ii) the mutated residue plays a central role in defining the relative ring rotation (of about 22 degrees) around the 7-fold axis; (iii) an increase in the inter-ring distance and solvent accessibility of the inter-ring interface; and (iv) a 2-fold reduction in the stabilization energy of the inter-ring interface, due to the modification of inter-ring interactions. These characteristics explain how the thermal sensitivity of the protein's fundamental properties permits GroEL to distinguish physiological (37 degrees C) from stress (42 degrees C) temperatures. | |||
Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K.,Cabo-Bilbao A, Spinelli S, Sot B, Agirre J, Mechaly AE, Muga A, Guerin DM J Struct Biol. 2006 Sep;155(3):482-92. Epub 2006 Jul 8. PMID:16904907<ref>PMID:16904907</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Chaperonin|Chaperonin]] | *[[Chaperonin|Chaperonin]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Agirre, J | [[Category: Agirre, J]] | ||
[[Category: Cabo-Bilbao, A | [[Category: Cabo-Bilbao, A]] | ||
[[Category: Guerin, D M.A | [[Category: Guerin, D M.A]] | ||
[[Category: Mechaly, A E | [[Category: Mechaly, A E]] | ||
[[Category: Muga, A | [[Category: Muga, A]] | ||
[[Category: Sot, B | [[Category: Sot, B]] | ||
[[Category: Spinelli, S | [[Category: Spinelli, S]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Chaperonin]] | [[Category: Chaperonin]] | ||
Revision as of 17:51, 21 December 2014
Crystal structure of the allosteric-defective chaperonin GroEL E434K mutant
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