4cqi: Difference between revisions

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'''Unreleased structure'''


The entry 4cqi is ON HOLD  until Paper Publication
==Crystal structure of recombinant tubulin-binding cofactor A (TBCA) from Leishmania major==
<StructureSection load='4cqi' size='340' side='right'caption='[[4cqi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cqi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CQI 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4cqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cqi OCA], [https://pdbe.org/4cqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cqi RCSB], [https://www.ebi.ac.uk/pdbsum/4cqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cqi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9U1D9_LEIMA Q9U1D9_LEIMA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tubulin-binding cofactor A (TBCA) participates in microtubule formation, a key process in eukaryotic biology to create the cytoskeleton. There is little information on how TBCA might interact with beta-tubulin en route to microtubule biogenesis. To address this, the protozoan Leishmania major was targeted as a model system. The crystal structure of TBCA and comparisons with three orthologous proteins are presented. The presence of conserved features infers that electrostatic interactions that are likely to involve the C-terminal tail of beta-tubulin are key to association. This study provides a reagent and template to support further work in this area.


Authors: Barrack, K.L., Fyfe, P.K., Hunter, W.N.
The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly.,Barrack KL, Fyfe PK, Hunter WN Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):539-46. doi:, 10.1107/S2053230X15000990. Epub 2015 Apr 21. PMID:25945706<ref>PMID:25945706</ref>


Description: Crystal structure of recombinant tubulin-binding cofactor A (TBCA) from Leishmania major
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cqi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leishmania major]]
[[Category: Barrack KL]]
[[Category: Fyfe PK]]
[[Category: Hunter WN]]
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