2eu1

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[[Image:2eu1.png|left|200px]]
[[Image:2eu1.png|left|200px]]
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{{STRUCTURE_2eu1| PDB=2eu1 | SCENE= }}
{{STRUCTURE_2eu1| PDB=2eu1 | SCENE= }}
===Crystal structure of the chaperonin GroEL-E461K===
===Crystal structure of the chaperonin GroEL-E461K===
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{{ABSTRACT_PUBMED_16904907}}
{{ABSTRACT_PUBMED_16904907}}
==About this Structure==
==About this Structure==
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[[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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[[2eu1]] is a 14 chain structure of [[Chaperonin]] and [[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].
==See Also==
==See Also==
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*[[Heat Shock Proteins]]
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*[[Chaperonin|Chaperonin]]
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*[[Heat Shock Proteins|Heat Shock Proteins]]
==Reference==
==Reference==
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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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<ref group="xtra">PMID:016904907</ref><ref group="xtra">PMID:016288915</ref><ref group="xtra">PMID:015475965</ref><ref group="xtra">PMID:008846220</ref><ref group="xtra">PMID:009285585</ref><ref group="xtra">PMID:016081650</ref><ref group="xtra">PMID:012110685</ref><ref group="xtra">PMID:012796493</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Agirre, J.]]
[[Category: Agirre, J.]]
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[[Category: Sot, B.]]
[[Category: Sot, B.]]
[[Category: Spinelli, S.]]
[[Category: Spinelli, S.]]
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[[Category: Chaperone/peptide binding protein complex]]
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[[Category: Chaperone-peptide binding protein complex]]
[[Category: Chaperonin]]
[[Category: Chaperonin]]
[[Category: E461k]]
[[Category: E461k]]
[[Category: Groel]]
[[Category: Groel]]
[[Category: Hsp60]]
[[Category: Hsp60]]

Revision as of 13:03, 26 July 2012

Image:2eu1.png

Template:STRUCTURE 2eu1

Contents

Crystal structure of the chaperonin GroEL-E461K

Template:ABSTRACT PUBMED 16904907

About this Structure

2eu1 is a 14 chain structure of Chaperonin and 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

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