From Proteopedia
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| | {{STRUCTURE_1rfl| PDB=1rfl | SCENE= }} | | {{STRUCTURE_1rfl| PDB=1rfl | SCENE= }} |
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| - | '''NMR data driven structural model of G-domain of MnmE protein'''
| + | ===NMR data driven structural model of G-domain of MnmE protein=== |
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| - | ==Overview==
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| - | The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well as on the formation of a MnmE transition state mimic. GTP hydrolysis by MnmE, but not GTP binding or formation of a complex with mant-GDP and aluminium fluoride, is impaired at acidic pH, suggesting that the chemistry of the transition state mimic is different to that of the true transition state, and that some residue(s), critical for GTP hydrolysis, is severely affected by low pH. We use a nuclear magnetic resonance (NMR)-based approach to get insights into the MnmE structure and properties. The combined use of NMR restraints and homology structural information allowed the determination of the MnmE G-domain structure in its free form. Chemical shift structure-based prediction provided a good basis for structure refinement and validation. Our data support that MnmE, unlike other GTPases, does not use an arginine finger to drive catalysis, although Arg252 may play a role in stabilization of the transition state. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17143896}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17143896 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17143896}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1RFL 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=1RFL OCA]. | + | 1RFL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFL OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Alpha/beta]] | | [[Category: Alpha/beta]] |
| | [[Category: Gtpase domain]] | | [[Category: Gtpase domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:26:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:20:04 2008'' |
Revision as of 00:20, 28 July 2008
Template:STRUCTURE 1rfl
NMR data driven structural model of G-domain of MnmE protein
Template:ABSTRACT PUBMED 17143896
About this Structure
1RFL is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.
Reference
Structural insights into the GTPase domain of Escherichia coli MnmE protein., Monleon D, Martinez-Vicente M, Esteve V, Yim L, Prado S, Armengod ME, Celda B, Proteins. 2007 Feb 15;66(3):726-39. PMID:17143896
Page seeded by OCA on Mon Jul 28 03:20:04 2008
