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2eu1

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==About this Structure==
==About this Structure==
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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].
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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].
==Reference==
==Reference==
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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]
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<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]]
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[[Category: Single protein]]
 
[[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''
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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 07:37, 17 February 2009

Image:2eu1.png

Template:STRUCTURE 2eu1

Crystal structure of the chaperonin GroEL-E461K

Template:ABSTRACT PUBMED 16904907

About this Structure

2EU1 is a 14 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

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

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