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| ==About this Structure== | | ==About this Structure== |
| 2EU1 is a [[Single protein]] structure of 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]. | | 2EU1 is a 14 chains structure of sequences 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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| ==Reference== | | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/16904907 16904907]
| | <ref group="xtra">PMID:16904907</ref><ref group="xtra">PMID:16288915</ref><ref group="xtra">PMID:15475965</ref><ref group="xtra">PMID:8846220</ref><ref group="xtra">PMID:9285585</ref><ref group="xtra">PMID:16081650</ref><ref group="xtra">PMID:12110685</ref><ref group="xtra">PMID:12796493</ref><references group="xtra"/> |
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/16288915 16288915]
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/15475965 15475965]
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/8846220 8846220]
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/9285585 9285585]
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/16081650 16081650]
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/12110685 12110685]
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/12796493 12796493]
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| [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| [[Category: Single protein]]
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| [[Category: Agirre, J.]] | | [[Category: Agirre, J.]] |
| [[Category: Cabo-Bilbao, A.]] | | [[Category: Cabo-Bilbao, A.]] |
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| [[Category: Hsp60]] | | [[Category: Hsp60]] |
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:14:43 2008'' | | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:37:21 2009'' |
