3mxz
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3mxz is ON HOLD Authors: Lu, Lu., Nan, Jie., Mi, Wei., Su, Xiao-Dong., Li, Yi. Description: Crystal Structure of tubulin folding cofactor A from Ar...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of tubulin folding cofactor A from Arabidopsis thaliana== | |
| + | <StructureSection load='3mxz' size='340' side='right'caption='[[3mxz]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3mxz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MXZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.599Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=3mxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mxz OCA], [https://pdbe.org/3mxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mxz RCSB], [https://www.ebi.ac.uk/pdbsum/3mxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mxz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mx/3mxz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mxz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:20638386</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3mxz" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Li Y]] | ||
| + | [[Category: Lu L]] | ||
| + | [[Category: Mi W]] | ||
| + | [[Category: Nan J]] | ||
| + | [[Category: Su XD]] | ||
Current revision
Crystal Structure of tubulin folding cofactor A from Arabidopsis thaliana
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Categories: Arabidopsis thaliana | Large Structures | Li Y | Lu L | Mi W | Nan J | Su XD
