PDBsum entry 6gwc

Cell cycle

PDB id: 6gwc

Contents

Protein chains

431 a.a.

417 a.a.

217 a.a.

Ligands

GTP ×2

PGE

MES ×2

Metals

_MG ×2

Waters ×176

PDB id:

6gwc

Name:

Cell cycle

Title:

Tubulin:ie5 alpharep complex

Structure:

Alpha-tubulin. Chain: a. Tubulin beta chain. Chain: b. Ie5 alpharep. Chain: c. Engineered: yes

Source:

Ovis aries. Organism_taxid: 9940. Sheep. Synthetic construct. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.60Å R-factor: 0.176 R-free: 0.223

Authors:

B.Gigant,V.Campanacci

Key ref:

V.Campanacci et al. (2019). Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit. Structure, 27, 497. PubMed id: 30661854 DOI: 10.1016/j.str.2018.12.001

Date:

22-Jun-18 Release date: 30-Jan-19

Protein chain

No UniProt id for this chain

Struc: 431 a.a.

Protein chain

D0VWY9  (D0VWY9_SHEEP) -  Tubulin beta chain from Ovis aries

Seq: 445 a.a.

Struc: 417 a.a.*

Protein chain

No UniProt id for this chain

Struc: 217 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain B: E.C.?

DOI no: 10.1016/j.str.2018.12.001

Structure 27:497 (2019)

PubMed id: 30661854

Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit.

V.Campanacci, A.Urvoas, T.Consolati, S.Cantos-Fernandes, M.Aumont-Nicaise, M.Valerio-Lepiniec, T.Surrey, P.Minard, B.Gigant.

ABSTRACT

Microtubules are cytoskeletal filaments of eukaryotic cells made of αβ-tubulin heterodimers. Structural studies of non-microtubular tubulin rely mainly on molecules that prevent its self-assembly and are used as crystallization chaperones. Here we identified artificial proteins from an αRep library that are specific to α-tubulin. Turbidity experiments indicate that these αReps impede microtubule assembly in a dose-dependent manner and total internal reflection fluorescence microscopy further shows that they specifically block growth at the microtubule (-) end. Structural data indicate that they do so by targeting the α-tubulin longitudinal surface. Interestingly, in one of the complexes studied, the α subunit is in a conformation that is intermediate between the ones most commonly observed in X-ray structures of tubulin and those seen in the microtubule, emphasizing the plasticity of tubulin. These α-tubulin-specific αReps broaden the range of tools available for the mechanistic study of microtubule dynamics and its regulation.