2bto: Difference between revisions
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<StructureSection load='2bto' size='340' side='right'caption='[[2bto]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2bto' size='340' side='right'caption='[[2bto]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bto]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2bto]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Prosthecobacter_dejongeii Prosthecobacter dejongeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BTO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bto OCA], [https://pdbe.org/2bto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bto RCSB], [https://www.ebi.ac.uk/pdbsum/2bto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bto ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bto OCA], [https://pdbe.org/2bto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bto RCSB], [https://www.ebi.ac.uk/pdbsum/2bto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bto ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q8GCC5_9BACT Q8GCC5_9BACT] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Prosthecobacter dejongeii]] | ||
[[Category: | [[Category: Lowe J]] | ||
[[Category: | [[Category: Schlieper D]] | ||
Revision as of 14:23, 22 May 2024
Structure of BtubA from Prosthecobacter dejongeiiStructure of BtubA from Prosthecobacter dejongeii
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedalphabeta-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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