PDBsum entry 2f6h

Structural protein

PDB id: 2f6h

Contents

Protein chain

390 a.a. *

Waters ×227

* Residue conservation analysis

PDB id:

2f6h

Name:

Structural protein

Title:

Myosin v cargo binding domain

Structure:

Myosin-2. Chain: x. Fragment: cargo binding domain. Synonym: class v unconventional myosin myo2. Type v myosin heavy chain myo2. Myosin v myo2. Cell division control protein 66. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: myo2, cdc66. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.25Å R-factor: 0.219 R-free: 0.250

Authors:

N.Pashkova,Y.Jin,S.Ramaswamy,L.S.Weisman

Key ref:

N.Pashkova et al. (2006). Structural basis for myosin V discrimination between distinct cargoes. EMBO J, 25, 693-700. PubMed id: 16437158 DOI: 10.1038/sj.emboj.7600965

Date:

29-Nov-05 Release date: 07-Feb-06

Protein chain

P19524  (MYO2_YEAST) -  Myosin-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1574 a.a.

Struc: 390 a.a.

DOI no: 10.1038/sj.emboj.7600965

EMBO J 25:693-700 (2006)

PubMed id: 16437158

Structural basis for myosin V discrimination between distinct cargoes.

N.Pashkova, Y.Jin, S.Ramaswamy, L.S.Weisman.

ABSTRACT

Myosin V molecular motors move cargoes on actin filaments. A myosin V may move multiple cargoes to distinct places at different times. The cargoes attach to the globular tail of myosin V via cargo-specific receptors. Here we report the crystal structure at 2.2 A of the myosin V globular tail. The overall tertiary structure has not been previously observed. There are several patches of highly conserved regions distributed on the surface of the tail. These are candidate attachment sites for cargo-specific receptors. Indeed, we identified a region of five conserved surface residues that are solely required for vacuole inheritance. Likewise, we identified a region of five conserved surface residues that are required for secretory vesicle movement, but not vacuole movement. These two regions are at opposite ends of the oblong-shaped cargo-binding domain, and moreover are offset by 180 degrees. The fact that the cargo-binding areas are distant from each other and simultaneously exposed on the surface of the globular tail suggests that major targets for the regulation of cargo attachment are organelle-specific myosin V receptors.

Selected figure(s)

Figure 1.
Figure 1 Structural overview of the Myo2p globular tail. (A) Ribbon representation of the structure in two orientations (rainbow colors from blue, N-terminus, to red, C-terminus). Vacuole-specific mutations D1297G/N, L1301P, N1304S, and N1307D/N are indicated in magenta. The most amino-terminal residue within the solved structure is 1152. (B) Topology diagram. Subdomain I is blue and subdomain II is red. Cyan indicates the region of the C-loop that is part of subdomain I. All structures presented in the figures were drawn using PyMol (DeLano Scientific LLC).

Figure 5.
Figure 5 The vacuole- and secretory vesicle-binding sites are structurally separated within the Myo2p globular tail. Surface residues of subdomain I are shown in blue and that of subdomain II in red. Vacuole-binding site is in cyan and secretory vesicle-specific site is in yellow. This present figure and Figure 3 show the same orientation.

The above figures are reprinted by permission from Macmillan Publishers Ltd: EMBO J (2006, 25, 693-700) copyright 2006.

Figures were selected by an automated process.