PDBsum entry 2of3

Structural protein, cell cycle

PDB id: 2of3

Contents

Protein chain

266 a.a. *

Waters ×229

* Residue conservation analysis

PDB id:

2of3

Name:

Structural protein, cell cycle

Title:

Tog domain structure from c.Elegans zyg9

Structure:

Zyg-9. Chain: a. Fragment: tog domain, residues 602-867. Synonym: hypothetical protein zyg-9. Engineered: yes

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Gene: zyg-9. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å R-factor: 0.175 R-free: 0.224

Authors:

J.Al-Bassam,N.A.Larsen,A.A.Hyman,S.C.Harrison

Key ref:

J.Al-Bassam et al. (2007). Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding. Structure, 15, 355-362. PubMed id: 17355870 DOI: 10.1016/j.str.2007.01.012

Date:

02-Jan-07 Release date: 13-Mar-07

Protein chain

G5EEM5  (ZYG9_CAEEL) -  Zygote defective protein 9 from Caenorhabditis elegans

Seq: 1415 a.a.

Struc: 266 a.a.

DOI no: 10.1016/j.str.2007.01.012

Structure 15:355-362 (2007)

PubMed id: 17355870

Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding.

J.Al-Bassam, N.A.Larsen, A.A.Hyman, S.C.Harrison.

ABSTRACT

Members of the XMAP215/Dis1 family of microtubule-associated proteins (MAPs) are essential for microtubule growth. MAPs in this family contain several 250 residue repeats, called TOG domains, which are thought to bind tubulin dimers and promote microtubule polymerization. We have determined the crystal structure of a single TOG domain from the Caenorhabditis elegans homolog, Zyg9, to 1.9 A resolution, and from it we describe a structural blueprint for TOG domains. These domains are flat, paddle-like structures, composed of six HEAT-repeat elements stacked side by side. The two wide faces of the paddle contain the HEAT-repeat helices, and the two narrow faces, the intra- and inter-HEAT repeat turns. Solvent-exposed residues in the intrarepeat turns are conserved, both within a particular protein and across the XMAP215/Dis1 family. Mutation of some of these residues in the TOG1 domain from the budding yeast homolog, Stu2p, shows that this face indeed participates in the tubulin contact.

Selected figure(s)

Figure 2.
Figure 2. Structure of Zyg9-TOG3
(A) Zyg9 TOG3 has seven HEAT repeats. HR0 contains helices 0A and 0B (red) linked by a 14 residue loop (T0). The six HEAT repeats that follow (blue helices, HR1–HR6) form the conserved TOG domain structure. In this view, the A helices (1A–6A) are in the front, the B helices (1B–6B), in the rear; turns between A and B helices of each repeat (T1–T6) are at the bottom, and interrepeat turns (T2-3 and T3-4) are at the top. The HR5 A helix is broken by a nonhelical linker into helices 5A1 and 5A2. HR6 packs onto HR5 with a right-handed 45° twist. There is a short β-ribbon (yellow strands, S0 and S1) at the N terminus.
(B) As in (A), but viewed from the bottom (structure rotated by 90°).
(C) As in (A), but structure rotated by 180°.

Figure 4.
Figure 4. Surface Representation of Zyg9-TOG3 Showing Conservation of Solvent-Exposed Residues on One Narrow Face of the Paddle-like Structure
Conserved, solvent-exposed residues are shown in the color scheme of Figure 3. (A) View as in Figure 1B. (B) View as in Figure 1C, showing the relative dimensions of the domain and of the conserved surface.

The above figures are reprinted by permission from Cell Press: Structure (2007, 15, 355-362) copyright 2007.

Figures were selected by an automated process.