PDBsum entry 2f77

Viral protein

PDB id: 2f77

Contents

Protein chain

100 a.a. *

* Residue conservation analysis

PDB id:

2f77

Name:

Viral protein

Title:

Solution structure of the r55f mutant of m-pmv matrix protein (p10)

Structure:

Core protein p10. Chain: x. Fragment: residues 1-100 of gag polyprotein. Synonym: m-pmv matrix protein. Engineered: yes. Mutation: yes. Other_details: a part of core polyprotein which contains: core protein p10. Core phosphoprotein pp18. Core protein p12. Core protein p27. Core protein p14. Core protein p4

Source:

Simian retrovirus 1. Organism_taxid: 11942. Gene: gag. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

18 models

Authors:

J.Vlach,J.Lipov,V.Veverka,J.Lang,P.Srb,M.Rumlova,E.Hunter,T.Ruml, R.Hrabal

Key ref:

J.Vlach et al. (2008). D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein. Proc Natl Acad Sci U S A, 105, 10565-10570. PubMed id: 18647839

Date:

30-Nov-05 Release date: 05-Dec-06

Protein chain

P07567  (GAG_MPMV) -  Gag polyprotein from Mason-Pfizer monkey virus

Seq: 657 a.a.

Struc: 100 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

Proc Natl Acad Sci U S A 105:10565-10570 (2008)

PubMed id: 18647839

D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.

J.Vlach, J.Lipov, M.Rumlová, V.Veverka, J.Lang, P.Srb, Z.Knejzlík, I.Pichová, E.Hunter, R.Hrabal, T.Ruml.

ABSTRACT

Despite extensive data demonstrating that immature retroviral particle assembly can take place either at the plasma membrane or at a distinct location within the cytoplasm, targeting of viral precursor proteins to either assembly site still remains poorly understood. Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site. Comparison of the three-dimensional structures of M-PMV wild-type matrix protein (wt MA) with a single amino acid mutant (R55F), which redirects assembly from a cytoplasmic site to the plasma membrane, revealed different mutual orientations of their C- and N-terminal domains. This conformational change buries a putative intracellular targeting motif located between both domains in the hydrophobic pocket of the MA molecule, thereby preventing the interaction with cellular transport mechanisms.