PDBsum entry: 1ffx

Structural protein

PDB id: 1ffx

Contents

Protein chains

423 a.a. *

410 a.a. *

91 a.a. *

Ligands

GTP ×2

GDP ×2

* Residue conservation analysis

PDB id:

1ffx

Name:

Structural protein

Title:

Tubulin:stathmin-like domain complex

Structure:

Protein (tubulin). Chain: a, c. Protein (tubulin). Chain: b, d. Protein (stathmin-like domain of rb3). Chain: e. Synonym: rb3. Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Organ: brain. Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Pentamer (from PQS)

Resolution:

3.95Å R-factor: 0.267 R-free: 0.367

Authors:

B.Gigant,C.Martin-Barbey,M.Knossow

Key ref:

B.Gigant et al. (2000). The 4 A X-ray structure of a tubulin:stathmin-like domain complex. Cell, 102, 809-816. PubMed id: 11030624 DOI: 10.1016/S0092-8674(00)00069-6

Date:

26-Jul-00 Release date: 27-Sep-00

Protein chains

P02550  (TBA1A_PIG) -  Tubulin alpha-1A chain

Seq: 451 a.a.

Struc: 423 a.a.

Protein chains

P02554  (TBB_PIG) -  Tubulin beta chain

Seq: 445 a.a.

Struc: 410 a.a.

Protein chain

No UniProt id for this chain

 Gene Ontology (GO) functional annotation 

• Cellular component: protein complex (2 terms)
• Biological process: microtubule-based process (4 terms)
• Biochemical function: structural molecule activity (4 terms)

DOI no: 10.1016/S0092-8674(00)00069-6

Cell 102:809-816 (2000)

PubMed id: 11030624

The 4 A X-ray structure of a tubulin:stathmin-like domain complex.

B.Gigant, P.A.Curmi, C.Martin-Barbey, E.Charbaut, S.Lachkar, L.Lebeau, S.Siavoshian, A.Sobel, M.Knossow.

ABSTRACT

Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics. The structure of the complex of GDP-tubulin with the stathmin-like domain of the neural protein RB3 reveals a head-to-tail assembly of two tubulins with a 91-residue RB3 alpha helix in which each copy of an internal duplicated sequence interacts with a different tubulin. As a result of the relative orientations adopted by tubulins and by their alpha and beta subunits, the tubulin:RB3 complex forms a curved structure. The RB3 helix thus most likely prevents incorporation of tubulin into microtubules by holding it in an assembly with a curvature very similar to that of the depolymerization products of microtubules.

Selected figure(s)

Figure 3.
Figure 3. The (T2R)[n] Structure Resulting from the Repetition of T2R which Illustrates the Curvature of This ComplexThis picture was obtained by superimposing the α[1]β[1] moiety of the m^th complex onto the α[2]β[2] moiety of the (m-1)^th complex and by keeping in the final structure (α[1]β[1])[1], (α[2]β[2])[1], (α[2]β[2])[2],…, (α[2]β[2])[n]. Each T2R complex, drawn as a Cα trace, is in a different color from its neighbors except the RB3-SLD helix which is in black. Top: view along the helix axis (noted as a cross); 8 complexes are represented. Bottom: view perpendicular to the helix axis, which is noted as a straight line; one turn of the helix, i.e., 8 T2R complexes, is represented.

Figure 4.
Figure 4. Comparison of T2R and Zinc Sheet Protofilament Tubulin(a) Schematic representation of the changes of the orientations of tubulin subunits in T2R as compared to straight protofilaments. The same colour code is used to identify tubulin subunits domains as in Figure 2. Nucleotides are represented as crosshatched blue (GDP) and red (GTP) motifs. T7 and H10 indicate the localizations of the T7 loop and of the H10 helix (intermediate domain, light green) that contact the neighboring subunit in Zn^2+ sheet protofilaments ([34]) (right) but not in T2R (left). The stathmin-like domain long α helix is represented by a thick dark blue line in T2R. The localizations of tubulin residues of the C-terminal domain and of the nucleotide binding domain that contact the stathmin-like domain long α helix are also noted (full circle and full oval, respectively). (b) Alignment of the RB3-SLD sequence with itself. The sequence alignment was performed with BLAST ( [2]), which detects 13 identities and 23 similarities over two 35-residue regions with a 16-residue gap. Only the regions of RB3-SLD with a significant sequence similarity are represented (top and bottom lines); identical residues and similarities (+) are plotted on the middle line. Residue numbering is as defined in Experimental Procedures. The sequence spacing of the stathmin-like domain residues with identical tubulin contacts is represented in (a) and corresponds to the spacing of the aligned stathmin-like domain residues.

The above figures are reprinted by permission from Cell Press: Cell (2000, 102, 809-816) copyright 2000.

Figures were selected by the author.