PDBsum entry 1ef1

Membrane protein

PDB id: 1ef1

Contents

Protein chains

294 a.a. *

90 a.a. *

Ligands

SO4 ×2

Waters ×412

* Residue conservation analysis

PDB id:

1ef1

Name:

Membrane protein

Title:

Crystal structure of the moesin ferm domain/tail domain complex

Structure:

Moesin. Chain: a, b. Fragment: n-terminal ferm domain. Engineered: yes. Moesin. Chain: c, d. Fragment: c-terminal tail domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Biol. unit:

Tetramer (from PQS)

Resolution:

1.90Å R-factor: 0.227 R-free: 0.287

Authors:

M.A.Pearson,D.Reczek,A.Bretscher,P.A.Karplus

Key ref:

M.A.Pearson et al. (2000). Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell, 101, 259-270. PubMed id: 10847681 DOI: 10.1016/S0092-8674(00)80836-3

Date:

04-Feb-00 Release date: 10-May-00

Protein chains

P26038  (MOES_HUMAN) -  Moesin from Homo sapiens

Seq: 577 a.a.

Struc: 294 a.a.

Protein chains

P26038  (MOES_HUMAN) -  Moesin from Homo sapiens

Seq: 577 a.a.

Struc: 90 a.a.

DOI no: 10.1016/S0092-8674(00)80836-3

Cell 101:259-270 (2000)

PubMed id: 10847681

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.

M.A.Pearson, D.Reczek, A.Bretscher, P.A.Karplus.

ABSTRACT

The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain, a common membrane binding module. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites. The crystal structure of a dormant moesin FERM/tail complex reveals that the FERM domain has three compact lobes including an integrated PTB/PH/ EVH1 fold, with the C-terminal segment bound as an extended peptide masking a large surface of the FERM domain. This extended binding mode suggests a novel mechanism for how different signals could produce varying levels of activation. Sequence conservation suggests a similar regulation of the tumor suppressor merlin.

Selected figure(s)

Figure 6.
Figure 6. Stereodiagram of the Region Surrounding Thr558Thr558 is in van der Waals contact with FERM residues Thr235 and Pro236, and is accessible to solvent from the right between the side chains of Arg553, Lys557, and Gln561. The electron density (from an NCS averaged map calculated with coefficients 2F[O] − 2F[C], αC) is contoured at 2.2 × ρ[rms]. A phosphoryl group modeled onto Thr558 collides with surrounding atoms from Arg553 and Gln561.

Figure 7.
Figure 7. Potential FERM Domain Interaction SitesThe positions of five binding sites on proteins that are structurally similar to the three FERM lobes are indicated: (1) by analogy with the protein interaction site seen for elongin B ([62]) and the Ras binding domain of Raf kinase ( [47]); (2) by analogy with the lipid binding site of the acyl CoA binding protein ( [36]), but this site is blocked by the loop connecting the F2 helices C and D; (3) by analogy with the proline-containing peptide binding site on EVH1 domains ( [53]; Federov et al., 1999); (4) by analogy with the canonical peptide binding site of PTB domains ( [74]); and (5) by analogy with the inositol phosphate binding sites on PH domains ( [13 and 31]).

The above figures are reprinted by permission from Cell Press: Cell (2000, 101, 259-270) copyright 2000.

Figures were selected by an automated process.