PDBsum entry 2d2s

Endocytosis/exocytosis

PDB id: 2d2s

Contents

Protein chain

217 a.a. *

* Residue conservation analysis

PDB id:

2d2s

Name:

Endocytosis/exocytosis

Title:

Crystal structure of the exo84p c-terminal domains

Structure:

Exocyst complex component exo84. Chain: a. Fragment: exo84p c-terminal domains. Synonym: exocyst complex protein of 84 kda, u1-snp1 associating protein 3. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.85Å R-factor: 0.269 R-free: 0.306

Authors:

G.Dong,A.H.Hutagalung,C.Fu,P.Novick,K.M.Reinisch

Key ref:

G.Dong et al. (2005). The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol, 12, 1094-1100. PubMed id: 16249794 DOI: 10.1038/nsmb1017

Date:

16-Sep-05 Release date: 01-Nov-05

Protein chain

P38261  (EXO84_YEAST) -  Exocyst complex component EXO84 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 753 a.a.

Struc: 217 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nsmb1017

Nat Struct Mol Biol 12:1094-1100 (2005)

PubMed id: 16249794

The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif.

G.Dong, A.H.Hutagalung, C.Fu, P.Novick, K.M.Reinisch.

ABSTRACT

The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a 160-A-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods.

Selected figure(s)

Figure 1.
Figure 1. Exo70p is a long rod composed of contiguous -helical bundles. (a) Ribbon diagram of Exo70p colored from blue at its N terminus to red at its C terminus. Domains A-D are indicated. (b) Exo70p colored according to electrostatic surface potential (on a scale from -15 kT to +15 kT), where blue is positive and red is negative. Exo70p is strikingly dipolar, with the N terminus negatively and the C terminus positively charged. The orientation on the left is as in a. Arrows indicate a conserved patch of arginine and lysine residues at the extreme C terminus of Exo70p (see Supplementary Fig. 2). (c) Sequence of Exo70p. Secondary structure elements are labeled as in a; helices that span domains are blue. Dotted lines represent regions in the crystal structure that are disordered. This figure was prepared using MolScript32 and GRASP (http://trantor.bioc.columbia.edu/grasp/)33.

Figure 5.
Figure 5. The structure of the Exo84p C terminus is similar to that of the Exo70p N terminus. (a) Exo84p C-terminal fragment (residues 523-753), colored from blue at residue 523 to red at residue 753. (b)Exo84 C-terminal fragment colored according to electrostatic surface potential (on a scale from -13 kT to +11 kT), where blue is positive and red is negative. The view on the left is as in a. (c) Exo70p N-terminal fragment (residues 67-341). (d) A superposition of the Exo84p C terminus (blue) and the Exo70p N terminus (pink) aligned using helices H1-H4 of Exo84p and H1-H3 and H5 of Exo70p (circled). The two helical bundles comprising the two protein fragments are differently oriented in Exo84p and Exo70p. The view is as in a and c. (e) A superposition of the Exo84p C terminus and the Exo70p N terminus aligned using helices H5-H9 of Exo84p and H6-H10 of Exo70p (circled). In the interest of clarity, the view is rotated with respect to that in d. Lsqman34 was used in the alignments in d and e. Figures were prepared with MolScript32 and GRASP33.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2005, 12, 1094-1100) copyright 2005.

Figures were selected by the author.