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2bto

From Proteopedia

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Revision as of 13:18, 24 November 2021

Structure of BtubA from Prosthecobacter dejongeii

Structural highlights

2bto is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Atcc 27091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
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, 2tir, 2trx, 2btq
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[THIO_ECOLI] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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.

References

↑ Schlieper D, Oliva MA, Andreu JM, Lowe J. Structure of bacterial tubulin BtubA/B: evidence for horizontal gene transfer. Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9170-5. Epub 2005 Jun 20. PMID:15967998

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bto"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bto' size='340' side='right'caption='[[2bto]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bto]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Atcc_27091 Atcc 27091]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BTO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bto]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [https://en.wikipedia.org/wiki/Atcc_27091 Atcc 27091]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>
+</td></tr><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f6m|1f6m]], [[1keb|1keb]], [[1m7t|1m7t]], [[1oaz|1oaz]], [[1skr|1skr]], [[1sks|1sks]], [[1skw|1skw]], [[1sl0|1sl0]], [[1sl1|1sl1]], [[1sl2|1sl2]], [[1srx|1srx]], [[1t7p|1t7p]], [[1t8e|1t8e]], [[1tho|1tho]], [[1tk0|1tk0]], [[1tk5|1tk5]], [[1tk8|1tk8]], [[1tkd|1tkd]], [[1txx|1txx]], [[1x9m|1x9m]], [[1x9s|1x9s]], [[1x9w|1x9w]], [[1xoa|1xoa]], [[1xob|1xob]], [[2tir|2tir]], [[2trx|2trx]], [[2btq|2btq]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f6m|1f6m]], [[1keb|1keb]], [[1m7t|1m7t]], [[1oaz|1oaz]], [[1skr|1skr]], [[1sks|1sks]], [[1skw|1skw]], [[1sl0|1sl0]], [[1sl1|1sl1]], [[1sl2|1sl2]], [[1srx|1srx]], [[1t7p|1t7p]], [[1t8e|1t8e]], [[1tho|1tho]], [[1tk0|1tk0]], [[1tk5|1tk5]], [[1tk8|1tk8]], [[1tkd|1tkd]], [[1txx|1txx]], [[1x9m|1x9m]], [[1x9s|1x9s]], [[1x9w|1x9w]], [[1xoa|1xoa]], [[1xob|1xob]], [[2tir|2tir]], [[2trx|2trx]], [[2btq|2btq]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bto OCA], [http://pdbe.org/2bto PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bto RCSB], [http://www.ebi.ac.uk/pdbsum/2bto PDBsum], [http://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>
 == Function ==
-[[http://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
+[[https://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
 *[[BtuB 3D structures|BtuB 3D structures]]
-*[[Thioredoxin|Thioredoxin]]
+*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
-*[[Tubulin|Tubulin]]
+*[[Tubulin 3D Structures|Tubulin 3D Structures]]
 == References ==
 <references/>

2bto

From Proteopedia

Revision as of 13:18, 24 November 2021

Structure of BtubA from Prosthecobacter dejongeii

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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