2eu1
From Proteopedia
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Crystal structure of the chaperonin GroEL-E461K
Overview
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.
About this Structure
2EU1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 10:08:31 2007
Categories: Escherichia coli | Single protein | Agirre, J. | Cabo-Bilbao, A. | Guerin, D.M.A. | Mechaly, A.E. | Muga, A. | Sot, B. | Spinelli, S. | Chaperonin | E461k | Groel | Hsp60
