PDBsum entry 3fqq

Metal binding protein

PDB id: 3fqq

Contents

Protein chains

160 a.a. *

Ligands

GOL

0BD

Metals

_ZN ×2

Waters ×203

* Residue conservation analysis

PDB id:

3fqq

Name:

Metal binding protein

Title:

Crystal structure of a novel dimeric form of hcv ns5a domain i protein

Structure:

Non-structural protein 5a. Chain: a, b. Fragment: hcv ns5a. Synonym: ns5a. Engineered: yes

Source:

Hepatitis c virus (isolate con1). Hcv. Organism_taxid: 333284. Strain: hcv genotype 1b. Subtype con1. Gene: nonstructural protein ns5a. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.222 R-free: 0.255

Authors:

R.A.Love

Key ref:

R.A.Love et al. (2009). Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus. J Virol, 83, 4395-4403. PubMed id: 19244328

Date:

07-Jan-09 Release date: 24-Mar-09

Protein chains

Q9WMX2  (POLG_HCVCO) -  Genome polyprotein from Hepatitis C virus genotype 1b (isolate Con1)

Seq: 3010 a.a.

Struc: 160 a.a.*

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

Enzyme reactions

• Enzyme class 1: E.C.2.7.7.48 - RNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
• Enzyme class 2: E.C.3.4.21.98 - hepacivirin.
• Reaction: Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
• Enzyme class 3: E.C.3.4.22.- - ?????
• Enzyme class 4: E.C.3.6.1.15 - nucleoside-triphosphate phosphatase.
• Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H⁺
• Enzyme class 5: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Virol 83:4395-4403 (2009)

PubMed id: 19244328

Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus.

R.A.Love, O.Brodsky, M.J.Hickey, P.A.Wells, C.N.Cronin.

ABSTRACT

A new protein expression vector design utilizing an N-terminal six-histidine tag and tobacco etch virus protease cleavage site upstream of the hepatitis C virus NS5A sequence has resulted in a more straightforward purification method and improved yields of purified NS5A domain I protein. High-resolution diffracting crystals of NS5A domain I (amino acids 33 to 202) [NS5A(33-202)] were obtained by using detergent additive crystallization screens, leading to the structure of a homodimer which is organized differently from that published previously (T. L. Tellinghuisen, J. Marcotrigiano, and C. M. Rice, Nature 435:374-379, 2005) yet is consistent with a membrane association model for NS5A. The monomer-monomer interface of NS5A(33-202) features an extensive buried surface area involving the most-highly conserved face of each monomer. The two alternate structural forms of domain I now available may be indicative of the multiple roles emerging for NS5A in viral RNA replication and viral particle assembly.