PDBsum entry 3pzd

Motor protein/apoptosis

PDB id: 3pzd

Contents

Protein chains

498 a.a. *

36 a.a. *

Ligands

GOL

Waters ×101

* Residue conservation analysis

PDB id:

3pzd

Name:

Motor protein/apoptosis

Title:

Structure of the myosin x myth4-ferm/dcc complex

Structure:

Myosin-x. Chain: a. Fragment: myth4-ferm tandem. Synonym: unconventional myosin-10. Engineered: yes. Netrin receptor dcc. Chain: b. Fragment: p3 motif. Synonym: tumor suppressor protein dcc.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kiaa0799, myo10. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Mouse. Organism_taxid: 10090.

Resolution:

2.50Å R-factor: 0.206 R-free: 0.259

Authors:

Z.Wei,J.Yan,L.Pan,M.Zhang

Key ref:

Z.Wei et al. (2011). Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain. Proc Natl Acad Sci U S A, 108, 3572-3577. PubMed id: 21321230

Date:

14-Dec-10 Release date: 23-Feb-11

Protein chain

Q9HD67  (MYO10_HUMAN) -  Unconventional myosin-X from Homo sapiens

Seq: 2058 a.a.

Struc: 498 a.a.*

Protein chain

P70211  (DCC_MOUSE) -  Netrin receptor DCC from Mus musculus

Seq: 1447 a.a.

Struc: 36 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Proc Natl Acad Sci U S A 108:3572-3577 (2011)

PubMed id: 21321230

Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain.

Z.Wei, J.Yan, Q.Lu, L.Pan, M.Zhang.

ABSTRACT

Myosin X (MyoX), encoded by Myo10, is a representative member of the MyTH4-FERM domain-containing myosins, and this family of unconventional myosins shares common functions in promoting formation of filopodia/stereocilia structures in many cell types with unknown mechanisms. Here, we present the structure of the MyoX MyTH4-FERM tandem in complex with the cytoplasmic tail P3 domain of the netrin receptor DCC. The structure, together with biochemical studies, reveals that the MyoX MyTH4 and FERM domains interact with each other, forming a structural and functional supramodule. Instead of forming an extended β-strand structure in other FERM binding targets, DCC_P3 forms a single α-helix and binds to the αβ-groove formed by β5 and α1 of the MyoX FERM F3 lobe. Structure-based amino acid sequence analysis reveals that the key polar residues forming the inter-MyTH4/FERM interface are absolutely conserved in all MyTH4-FERM tandem-containing proteins, suggesting that the supramodular nature of the MyTH4-FERM tandem is likely a general property for all MyTH4-FERM proteins.