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2BTQ

Structure of BtubAB heterodimer from Prosthecobacter dejongeii

Summary for 2BTQ
Entry DOI10.2210/pdb2btq/pdb
Related2BTO
DescriptorTUBULIN BTUBA, TUBULIN BTUBB, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsstructural protein, cytoskeletal protein-complex, bacterial tubulin, cytoskeleton, polymerization, verrucomicrobia, protein complex, cytoskeletal protein
Biological sourcePROSTHECOBACTER DEJONGEII
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Total number of polymer chains2
Total formula weight98592.33
Authors
Schlieper, D.,Lowe, J. (deposition date: 2005-06-06, release date: 2005-06-14, Last modification date: 2023-12-13)
Primary citationSchlieper, 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: 15967998
DOI: 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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数据于2024-11-06公开中

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