PDBsum entry 2i1j

Cell adhesion, membrane protein

PDB id: 2i1j

Contents

Protein chain

481 a.a. *

Ligands

URE ×2

GOL ×3

Metals

_CL

Waters ×411

* Residue conservation analysis

PDB id:

2i1j

Name:

Cell adhesion, membrane protein

Title:

Moesin from spodoptera frugiperda at 2.1 angstroms resolution

Structure:

Moesin. Chain: a

Source:

Spodoptera frugiperda. Fall armyworm. Organism_taxid: 7108

Resolution:

2.10Å R-factor: 0.176 R-free: 0.215

Authors:

Q.Li,M.R.Nance,J.J.G.Tesmer

Key ref:

Q.Li et al. (2007). Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain. J Mol Biol, 365, 1446-1459. PubMed id: 17134719 DOI: 10.1016/j.jmb.2006.10.075

Date:

14-Aug-06 Release date: 19-Dec-06

Protein chain

A0T1L9  (A0T1L9_SPOFR) -  Moesin/ezrin/radixin homolog 1 from Spodoptera frugiperda

Seq: 575 a.a.

Struc: 481 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2006.10.075

J Mol Biol 365:1446-1459 (2007)

PubMed id: 17134719

Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain.

Q.Li, M.R.Nance, R.Kulikauskas, K.Nyberg, R.Fehon, P.A.Karplus, A.Bretscher, J.J.Tesmer.

ABSTRACT

Ezrin/radixin/moesin (ERM) family members provide a regulated link between the cortical actin cytoskeleton and the plasma membrane to govern membrane structure and organization. Here, we report the crystal structure of intact insect moesin, revealing that its essential yet previously uncharacterized alpha-helical domain forms extensive interactions with conserved surfaces of the band four-point-one/ezrin/radixin/moesin (FERM) domain. These interdomain contacts provide a functional explanation for how PIP(2) binding and tyrosine phosphorylation of ezrin lead to activation, and provide an understanding of previously enigmatic loss-of-function missense mutations in the tumor suppressor merlin. Sequence conservation and biochemical results indicate that this structure represents a complete model for the closed state of all ERM-merlin proteins, wherein the central alpha-helical domain is an active participant in an extensive set of inhibitory interactions that can be unmasked, in a rheostat-like manner, by coincident regulatory factors that help determine cell polarity and membrane structure.

Selected figure(s)

Figure 2.
Figure 2. Comparison of dormant human and Sfmoesin structures. (a) The human FERM–C-terminal domain complex (PDB code 1EF1). The three lobes of the ERM domain (F1, F2 and F3) are colored cyan and the C-terminal domain is colored red. The β1 strand of the C-terminal domain is contributed by a crystal-packing interaction. (b) The 2.1 Å Sfmoesin structure. The α-helical domain (yellow) folds into three extended helices (αA, αB and αC), each containing elements that pack against the FERM domain. The αB and αC helices form an anti-parallel coiled-coil. (c) In the 3.0 Å structure, 67 more residues of the vert, similar 70 Å αB/αC coiled-coil are revealed. Figure 2. Comparison of dormant human and Sfmoesin structures. (a) The human FERM–C-terminal domain complex (PDB code 1EF1). The three lobes of the ERM domain (F1, F2 and F3) are colored cyan and the C-terminal domain is colored red. The β1 strand of the C-terminal domain is contributed by a crystal-packing interaction. (b) The 2.1 Å Sfmoesin structure. The α-helical domain (yellow) folds into three extended helices (αA, αB and αC), each containing elements that pack against the FERM domain. The αB and αC helices form an anti-parallel coiled-coil. (c) In the 3.0 Å structure, 67 more residues of the [3]not, vert, similar 70 Å αB/αC coiled-coil are revealed.

Figure 4.
Figure 4. Extent and sequence conservation of the surfaces buried by the α-helical domain and linker region. (a) The Sfmoesin FERM domain. The view is rotated by vert, similar 180° around a vertical axis from that in Figure 2. (b) Molecular surface of the FERM domain. Yellow regions are those in contact with the α-helical domain and linker region ( vert, similar 1800 Å^2 of buried accessible surface area). (c) Conservation of the FERM domain. Magenta regions correspond to residues that are either identical or substituted conservatively (e.g. Asp/Glu, Arg/Lys, Ser/Thr) in all ERM-merlin proteins. Green regions correspond to residues conserved only in the ERM family. Figure 4. Extent and sequence conservation of the surfaces buried by the α-helical domain and linker region. (a) The Sfmoesin FERM domain. The view is rotated by [3]not, vert, similar 180° around a vertical axis from that in [4]Figure 2. (b) Molecular surface of the FERM domain. Yellow regions are those in contact with the α-helical domain and linker region ( [5]not, vert, similar 1800 Å^2 of buried accessible surface area). (c) Conservation of the FERM domain. Magenta regions correspond to residues that are either identical or substituted conservatively (e.g. Asp/Glu, Arg/Lys, Ser/Thr) in all ERM-merlin proteins. Green regions correspond to residues conserved only in the ERM family.

The above figures are reprinted from an Open Access publication published by Elsevier: J Mol Biol (2007, 365, 1446-1459) copyright 2007.

Figures were selected by the author.