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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Rice, David W. Muench, Stephen P. Sedelnikova, Svetlana E. Xu, Ling |
| Description | Author Affiliation: Muench SP ( Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom.); |
| Abstract | The structure of a Bacillus subtilis YphC/GDP complex shows that it contains two GTPase domains that pack against a central domain whose fold resembles that of an RNA binding KH-domain. Comparisons of this structure to that of a homologue in Thermotoga maritima reveals a dramatic rearrangement in the position of the N-terminal GTPase domain with a shift of up to 60 A and the formation of a totally different interface to the central domain. This rearrangement appears to be triggered by conformational changes of the switch II region in this domain in response to nucleotide binding. Modeling studies suggest that this motion represents transitions between the 'on' and 'off' states of the GTPase, the effect of which is to alternately expose and bury a positively charged face of the central domain that we suggest is involved in RNA recognition as part of the possible role of this enzyme in ribosome binding. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 33 |
| Volume Number | 103 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2006-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacillus Subtilis Enzymology Bacterial Proteins Chemistry GTP Phosphohydrolases Nucleotides Metabolism Protein Structure, Tertiary Amino Acid Sequence Genetics Guanosine Diphosphate Models, Molecular Molecular Sequence Data Protein Binding Sequence Alignment Thermotoga Maritima Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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