2eu1

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Image:2eu1.png

Template:STRUCTURE 2eu1

Crystal structure of the chaperonin GroEL-E461K

Template:ABSTRACT PUBMED 16904907

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

Crystal structure of wild-type chaperonin GroEL., Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H, J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:16288915

A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation., Sewell BT, Best RB, Chen S, Roseman AM, Farr GW, Horwich AL, Saibil HR, Nat Struct Mol Biol. 2004 Nov;11(11):1128-33. Epub 2004 Oct 10. PMID:15475965

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution., Braig K, Adams PD, Brunger AT, Nat Struct Biol. 1995 Dec;2(12):1083-94. PMID:8846220

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex., Xu Z, Horwich AL, Sigler PB, Nature. 1997 Aug 21;388(6644):741-50. PMID:9285585

Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study., Sot B, von Germar F, Mantele W, Valpuesta JM, Taneva SG, Muga A, Protein Sci. 2005 Sep;14(9):2267-74. Epub 2005 Aug 4. PMID:16081650

Salt bridges at the inter-ring interface regulate the thermostat of GroEL., Sot B, Galan A, Valpuesta JM, Bertrand S, Muga A, J Biol Chem. 2002 Sep 13;277(37):34024-9. Epub 2002 Jul 10. PMID:12110685

GroEL stability and function. Contribution of the ionic interactions at the inter-ring contact sites., Sot B, Banuelos S, Valpuesta JM, Muga A, J Biol Chem. 2003 Aug 22;278(34):32083-90. Epub 2003 Jun 9. PMID:12796493

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