2BTO
Structure of BtubA from Prosthecobacter dejongeii
Summary for 2BTO
Entry DOI | 10.2210/pdb2bto/pdb |
Related | 1F6M 1KEB 1M7T 1OAZ 1SKR 1SKS 1SKW 1SL0 1SL1 1SL2 1SRX 1T7P 1T8E 1THO 1TK0 1TK5 1TK8 1TKD 1TXX 1X9M 1X9S 1X9W 1XOA 1XOB 2BTQ 2TIR 2TRX |
Descriptor | TUBULIN BTUBA, THIOREDOXIN 1, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | bacterial tubulin, polymerization, cytoskeleton, protein complex, cytoskeletal protein |
Biological source | PROSTHECOBACTER DEJONGEII More |
Total number of polymer chains | 3 |
Total formula weight | 115332.49 |
Authors | Schlieper, D.,Lowe, J. (deposition date: 2005-06-04, release date: 2005-06-23, Last modification date: 2024-10-16) |
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 (2.5 Å) |
Structure validation
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