2bto
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STRUCTURE OF BTUBA FROM PROSTHECOBACTER DEJONGEII
OverviewOverview
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.
About this StructureAbout this Structure
2BTO is a Protein complex structure of sequences from Escherichia coli and Prosthecobacter dejongeii with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structure of bacterial tubulin BtubA/B: evidence for horizontal gene transfer., Schlieper D, Oliva MA, Andreu JM, Lowe J, Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9170-5. Epub 2005 Jun 20. PMID:15967998
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