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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2006-6-22
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pubmed:abstractText |
MnmE, a Guanine nucleotide-binding protein conserved between bacteria and man, is involved in the modification of tRNAs. Here we provide biochemical and X-ray structural evidence for a new GTP-hydrolysis mechanism, where the G-domains of MnmE dimerise in a potassium-dependent manner and induce GTP hydrolysis. The structure in the presence of GDP-AlFx and potassium shows how juxtaposition of the subunits induces a conformational change around the nucleotide which reorients the catalytic machinery. A critical glutamate is positioned such as to stabilise or activate the attacking water. Potassium provides a positive charge into the catalytic site in a position analogous to the arginine finger in the Ras-RasGAP system. Mutational studies show that potassium-dependent dimerisation and GTP hydrolysis can be uncoupled and that interaction between the G-domains is a prerequisite for subsequent phosphoryl transfer. We propose a model for the juxtaposition of G-domains in the full-length protein and how it induces conformational changes in the putative tRNA-modification centre.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16763562-10222271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16763562-10376676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16763562-10508770,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16763562-9811540
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2940-51
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16763562-Aluminum Compounds,
pubmed-meshheading:16763562-Amino Acid Sequence,
pubmed-meshheading:16763562-Binding Sites,
pubmed-meshheading:16763562-Catalysis,
pubmed-meshheading:16763562-Crystallography, X-Ray,
pubmed-meshheading:16763562-Dimerization,
pubmed-meshheading:16763562-Enzyme Activation,
pubmed-meshheading:16763562-Escherichia coli,
pubmed-meshheading:16763562-Escherichia coli Proteins,
pubmed-meshheading:16763562-Fluorides,
pubmed-meshheading:16763562-GTP Phosphohydrolases,
pubmed-meshheading:16763562-Models, Molecular,
pubmed-meshheading:16763562-Molecular Sequence Data,
pubmed-meshheading:16763562-Mutation,
pubmed-meshheading:16763562-Nucleotides,
pubmed-meshheading:16763562-Potassium,
pubmed-meshheading:16763562-Protein Binding,
pubmed-meshheading:16763562-Protein Structure, Quaternary
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pubmed:year |
2006
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pubmed:articleTitle |
Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element.
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pubmed:affiliation |
Max-Planck-Institut für Molekulare Physiologie, Dortmund, Germany.
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