4cqi

Crystal structure of recombinant tubulin-binding cofactor A (TBCA) from Leishmania major

spinqualitylabelsall models 4cqi, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cqi is a 1 chain structure with sequence from Leishmania major. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9U1D9_LEIMA 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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