2BTQ
Structure of BtubAB heterodimer from Prosthecobacter dejongeii
Summary for 2BTQ
Entry DOI | 10.2210/pdb2btq/pdb |
Related | 2BTO |
Descriptor | TUBULIN BTUBA, TUBULIN BTUBB, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | structural protein, cytoskeletal protein-complex, bacterial tubulin, cytoskeleton, polymerization, verrucomicrobia, protein complex, cytoskeletal protein |
Biological source | PROSTHECOBACTER DEJONGEII More |
Total number of polymer chains | 2 |
Total formula weight | 98592.33 |
Authors | Schlieper, D.,Lowe, J. (deposition date: 2005-06-06, release date: 2005-06-14, Last modification date: 2023-12-13) |
Primary citation | Schlieper, D.,Oliva, M.A.,Andreu, J.M.,Lowe, J. Structure of Bacterial Tubulin Btuba/B: Evidence for Horizontal Gene Transfer. Proc.Natl.Acad.Sci.USA, 102:9170-, 2005 Cited by PubMed Abstract: alphabeta-Tubulin heterodimers, from which the microtubules of the cytoskeleton are built, have a complex chaperone-dependent folding pathway. They are thought to be unique to eukaryotes, whereas the homologue FtsZ can be found in bacteria. The exceptions are BtubA and BtubB from Prosthecobacter, which have higher sequence homology to eukaryotic tubulin than to FtsZ. Here we show that some of their properties are different from tubulin, such as weak dimerization and chaperone-independent folding. However, their structure is strikingly similar to tubulin including surface loops, and BtubA/B form tubulin-like protofilaments. Presumably, BtubA/B were transferred from a eukaryotic cell by horizontal gene transfer because their high degree of similarity to eukaryotic genes is unique within the Prosthecobacter genome. PubMed: 15967998DOI: 10.1073/PNAS.0502859102 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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