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| - | [[Image:1skq.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1skq| PDB=1skq | SCENE= }} | | {{STRUCTURE_1skq| PDB=1skq | SCENE= }} |
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| - | '''The crystal structure of Sulfolobus solfataricus elongation factor 1-alpha in complex with magnesium and GDP'''
| + | ===The crystal structure of Sulfolobus solfataricus elongation factor 1-alpha in complex with magnesium and GDP=== |
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| - | ==Overview==
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| - | Recent studies have shown that elongation factors extracted from archaea/eukarya and from eubacteria exhibit different structural and functional properties. Along this line, it has been demonstrated that, in contrast to EF-Tu, Sulfolobus solfataricus EF-1alpha in complex with GDP (SsEF-1alpha.GDP) does not bind Mg(2+), when the ion is present in the crystallization medium at moderate concentration (5 mM). To further investigate the role that magnesium plays in the exchange process of EF-1alpha and to check the ability of SsEF-1alpha.GDP to bind the ion, we have determined the crystal structure of SsEF-1alpha.GDP in the presence of a nonphysiological concentration (100 mM) of Mg(2+). The analysis of the coordination of Mg(2+) unveils the structural bases for the marginal role played by the ion in the nucleotide exchange process. Furthermore, nucleotide exchange experiments carried out on a truncated form of SsEF-1alpha, consisting only of the nucleotide binding domain, demonstrate that the low affinity of SsEF-1alpha.GDP for Mg(2+) is due to the local architecture of the active site and does not depend on the presence of the other two domains. Finally, considering the available structures of EF-1alpha, a detailed mechanism for the nucleotide exchange process has been traced. Notably, this mechanism involves residues such as His14, Arg95, Gln131, and Glu134, which are strictly conserved in all archaea and eukarya EF-1alpha sequences hitherto reported.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15157096}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15157096 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15157096}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Elongation factor]] | | [[Category: Elongation factor]] |
| | [[Category: Protein synthesis]] | | [[Category: Protein synthesis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:49:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:40:17 2008'' |
Revision as of 17:40, 27 July 2008
Template:STRUCTURE 1skq
The crystal structure of Sulfolobus solfataricus elongation factor 1-alpha in complex with magnesium and GDP
Template:ABSTRACT PUBMED 15157096
About this Structure
1SKQ is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with magnesium and GDP., Vitagliano L, Ruggiero A, Masullo M, Cantiello P, Arcari P, Zagari A, Biochemistry. 2004 Jun 1;43(21):6630-6. PMID:15157096
Page seeded by OCA on Sun Jul 27 20:40:17 2008
