2bto

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[[Image:2bto.gif|left|200px]]
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{{STRUCTURE_2bto| PDB=2bto | SCENE= }}
{{STRUCTURE_2bto| PDB=2bto | SCENE= }}
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'''STRUCTURE OF BTUBA FROM PROSTHECOBACTER DEJONGEII'''
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===STRUCTURE OF BTUBA FROM PROSTHECOBACTER DEJONGEII===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15967998 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15967998}}
==About this Structure==
==About this Structure==
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[[Category: Polymerization]]
[[Category: Polymerization]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:47:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:38:57 2008''

Revision as of 14:38, 28 July 2008

Template:STRUCTURE 2bto

STRUCTURE OF BTUBA FROM PROSTHECOBACTER DEJONGEII

Template:ABSTRACT PUBMED 15967998

About this Structure

2BTO is a Protein complex structure of sequences from Escherichia coli and Prosthecobacter dejongeii. Full crystallographic information is available from OCA.

Reference

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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