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2eu1
From Proteopedia
(Difference between revisions)
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[[Image:2eu1.png|left|200px]] | [[Image:2eu1.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2eu1]] is a 14 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EU1 OCA]. | |
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| + | ==See Also== | ||
| + | *[[Heat Shock Proteins]] | ||
==Reference== | ==Reference== | ||
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[[Category: Sot, B.]] | [[Category: Sot, B.]] | ||
[[Category: Spinelli, S.]] | [[Category: Spinelli, S.]] | ||
| + | [[Category: Chaperone/peptide binding protein complex]] | ||
[[Category: Chaperonin]] | [[Category: Chaperonin]] | ||
[[Category: E461k]] | [[Category: E461k]] | ||
[[Category: Groel]] | [[Category: Groel]] | ||
[[Category: Hsp60]] | [[Category: Hsp60]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:37:21 2009'' | ||
Revision as of 00:16, 15 March 2011
Contents |
Crystal structure of the chaperonin GroEL-E461K
Template:ABSTRACT PUBMED 16904907
About this Structure
2eu1 is a 14 chain structure of Heat Shock Proteins with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Cabo-Bilbao A, Spinelli S, Sot B, Agirre J, Mechaly AE, Muga A, Guerin DM. Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K. J Struct Biol. 2006 Sep;155(3):482-92. Epub 2006 Jul 8. PMID:16904907 doi:10.1016/j.jsb.2006.06.008
- Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H. Crystal structure of wild-type chaperonin GroEL. J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:16288915 doi:10.1016/j.jmb.2005.09.096
- Sewell BT, Best RB, Chen S, Roseman AM, Farr GW, Horwich AL, Saibil HR. A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation. Nat Struct Mol Biol. 2004 Nov;11(11):1128-33. Epub 2004 Oct 10. PMID:15475965 doi:10.1038/nsmb844
- Braig K, Adams PD, Brunger AT. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution. Nat Struct Biol. 1995 Dec;2(12):1083-94. PMID:8846220
- Xu Z, Horwich AL, Sigler PB. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 1997 Aug 21;388(6644):741-50. PMID:9285585 doi:http://dx.doi.org/10.1038/41944
- Sot B, von Germar F, Mantele W, Valpuesta JM, Taneva SG, Muga A. Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study. Protein Sci. 2005 Sep;14(9):2267-74. Epub 2005 Aug 4. PMID:16081650 doi:10.1110/ps.051469605
- Sot B, Galan A, Valpuesta JM, Bertrand S, Muga A. Salt bridges at the inter-ring interface regulate the thermostat of GroEL. J Biol Chem. 2002 Sep 13;277(37):34024-9. Epub 2002 Jul 10. PMID:12110685 doi:10.1074/jbc.M205733200
- Sot B, Banuelos S, Valpuesta JM, Muga A. GroEL stability and function. Contribution of the ionic interactions at the inter-ring contact sites. J Biol Chem. 2003 Aug 22;278(34):32083-90. Epub 2003 Jun 9. PMID:12796493 doi:10.1074/jbc.M303958200
