PDBsum entry: 1dsv

Viral protein

PDB id: 1dsv

Contents

Protein chain

31 a.a. *

Metals

_ZN

* Residue conservation analysis

PDB id:

1dsv

Name:

Viral protein

Title:

Structure of the mmtv nucleocapsid protein (c-terminal zinc finger)

Structure:

Nucleic acid binding protein p14. Chain: a. Fragment: c-terminal zinc finger of nucleocapsid protein. Engineered: yes

Source:

Mouse mammary tumor virus. Organism_taxid: 11757. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

D.J.Klein,P.E.Johnson,E.S.Zollars,R.N.De Guzman,M.F.Summers

Key ref:

D.J.Klein et al. (2000). The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle. Biochemistry, 39, 1604-1612. PubMed id: 10677209 DOI: 10.1021/bi9922493

Date:

08-Jan-00 Release date: 28-Jan-00

Protein chain

P11284  (GAG_MMTVC) -  Gag polyprotein

Seq: 591 a.a.

Struc: 31 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: nucleic acid binding (2 terms)

DOI no: 10.1021/bi9922493

Biochemistry 39:1604-1612 (2000)

PubMed id: 10677209

The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle.

D.J.Klein, P.E.Johnson, E.S.Zollars, R.N.De Guzman, M.F.Summers.

ABSTRACT

The nucleocapsid protein (NC) from the mouse mammary tumor virus (MMTV) has been overexpressed in Escherichia coli and purified to homogeneity for structural studies by nuclear magnetic resonance (NMR) spectroscopy. The protein contains two copies of a conserved zinc-coordinating "CCHC array" or "zinc knuckle" motif common to the nucleocapsid proteins of nearly all known retroviruses. The residues comprising and adjacent to the zinc knuckles were assigned by standard two-dimensional (1)H and three-dimensional (1)H-(15)N NMR methods; the rotational dynamic properties of the protein were determined from (15)N relaxation experiments, and distance restraints derived from the nuclear Overhauser effect (NOE) data were used to calculate the three-dimensional structure. The (1)H-(1)H NOE and (15)N relaxation data indicate that the two zinc knuckles do not interact with each other, but instead behave as independently folded domains connected by a flexible 13-residue linker segment. The proximal zinc knuckle folds in a manner that is essentially identical to that observed previously for the two zinc knuckles of the human immunodeficiency virus type 1 nucleocapsid protein and for the moloney murine leukemia virus nucleocapsid zinc knuckle domain. However, the distal zinc knuckle of MMTV NC exhibits a rare three-dimensional fold that includes an additional C-terminal beta-hairpin. A similar C-terminal reverse turn-like structure was observed recently in the distal zinc knuckle of the Mason-Pfizer monkey virus nucleocapsid protein [Gao, Y., et al. (1998) Protein Sci. 7, 2265-2280]. However, despite a high degree of sequence homology, the conformation and orientation of the beta-hairpin in MMTV NC is significantly different from that of the reverse turn in MPMV NC. The results support the conclusion that structural features of NC zinc knuckle domains can vary significantly among the different genera of retroviridae, and are discussed in terms of the recent and surprising discovery that MMTV NC can facilitate packaging of the HIV-1 genome in chimeric MMTV mutants.