2eu1

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{{STRUCTURE_2eu1| PDB=2eu1 | SCENE= }}
{{STRUCTURE_2eu1| PDB=2eu1 | SCENE= }}
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'''Crystal structure of the chaperonin GroEL-E461K'''
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===Crystal structure of the chaperonin GroEL-E461K===
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==Overview==
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The chaperonin GroEL adopts a double-ring structure with various modes of allosteric communication. The simultaneous positive intra-ring and negative inter-ring co-operativities alternate the functionality of the folding cavities in both protein rings. Negative inter-ring co-operativity is maintained through different inter-ring interactions, including a salt bridge involving Glu 461. Replacement of this residue by Lys modifies the temperature sensitivity of the substrate-folding activity of this protein, most likely as a result of the loss of inter-ring co-operativity. The crystal structure of the mutant chaperonin GroELE461K has been determined at 3.3A and compared with other structures: the wild-type GroEL, an allosteric defective GroEL double mutant and the GroEL-GroES-(ADP)7 complex. The inter-ring region of the mutant exhibits the following characteristics: (i) no salt-bridge stabilizes the inter-ring interface; (ii) the mutated residue plays a central role in defining the relative ring rotation (of about 22 degrees) around the 7-fold axis; (iii) an increase in the inter-ring distance and solvent accessibility of the inter-ring interface; and (iv) a 2-fold reduction in the stabilization energy of the inter-ring interface, due to the modification of inter-ring interactions. These characteristics explain how the thermal sensitivity of the protein's fundamental properties permits GroEL to distinguish physiological (37 degrees C) from stress (42 degrees C) temperatures.
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The line below this paragraph, {{ABSTRACT_PUBMED_16904907}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16904907 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16904907}}
==About this Structure==
==About this Structure==
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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]
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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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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Groel]]
[[Category: Groel]]
[[Category: Hsp60]]
[[Category: Hsp60]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:06:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:14:43 2008''

Revision as of 10:14, 28 July 2008

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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