3mxz

From Proteopedia

(Difference between revisions)

Revision as of 12:24, 25 December 2014

Crystal Structure of tubulin folding cofactor A from Arabidopsis thaliana

Structural highlights

3mxz is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	KIS (Arabidopsis thaliana)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TBCA_ARATH] Tubulin-folding protein; involved in the early step of the tubulin folding pathway (By similarity).

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

Microtubules are composed of polymerized alpha/beta-tubulin heterodimers. Biogenesis of assembly-competent tubulin dimers is a complex multistep process that requires sequential actions of distinct molecular chaperones and cofactors. Tubulin folding cofactor A (TFCA), which captures beta-tubulin during the folding pathway, has been identified in many organisms. Here, we report the crystal structure of Arabidopsis thaliana TFC A (KIESEL, KIS), which forms a monomeric three-helix bundle. The functional binding analysis demonstrated that KIS interacts with beta-tubulin in plant. Furthermore, mutagenesis studies indicated that the alpha-helical regions of KIS participate in beta-tubulin binding. Unlike the budding yeast TFC A, the two loop regions of KIS are not required for this interaction suggesting a distinct binding mechanism of TFC A to beta-tubulin in plants.

Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization.,Lu L, Nan J, Mi W, Li LF, Wei CH, Su XD, Li Y FEBS Lett. 2010 Aug 20;584(16):3533-9. Epub 2010 Jul 16. PMID:20638386^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lu L, Nan J, Mi W, Li LF, Wei CH, Su XD, Li Y. Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization. FEBS Lett. 2010 Aug 20;584(16):3533-9. Epub 2010 Jul 16. PMID:20638386 doi:10.1016/j.febslet.2010.07.017

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3mxz"

@@ Line 7: / Line 7: @@
 <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=3mxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mxz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mxz RCSB], [http://www.ebi.ac.uk/pdbsum/3mxz PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TBCA_ARATH TBCA_ARATH]] Tubulin-folding protein; involved in the early step of the tubulin folding pathway (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3mxz

From Proteopedia

Revision as of 12:24, 25 December 2014

Crystal Structure of tubulin folding cofactor A from Arabidopsis thaliana

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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