PDBsum entry 2kys

Viral protein

PDB id: 2kys

Contents

Protein chain

85 a.a. *

* Residue conservation analysis

PDB id:

2kys

Name:

Viral protein

Title:

Nmr structure of the sars coronavirus nonstructural protein nsp7 in solution at ph 6.5

Structure:

Non-structural protein 7. Chain: a. Synonym: nsp7. Engineered: yes

Source:

Sars coronavirus. Organism_taxid: 227859. Strain: tor2. Gene: 1a. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

M.A.Johnson,K.Jaudzems,I.A.Wilson,K.Wuthrich,Joint Center For Structural Genomics (Jcsg)

Key ref:

M.A.Johnson et al. (2010). NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5. J Mol Biol, 402, 619-628. PubMed id: 20709084

Date:

07-Jun-10 Release date: 16-Jun-10

Protein chain

P0C6U8  (R1A_CVHSA) -  Replicase polyprotein 1a from Severe acute respiratory syndrome coronavirus

Seq: 4382 a.a.

Struc: 85 a.a.*

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

Enzyme reactions

• Enzyme class 1: E.C.2.7.7.50 - mRNA guanylyltransferase.
• Reaction: a 5'-end diphospho-ribonucleoside in mRNA + GTP + H⁺ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate
• Enzyme class 2: E.C.3.4.19.12 - ubiquitinyl hydrolase 1.
• Reaction: Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
• Enzyme class 3: E.C.3.4.22.- - ?????
• Enzyme class 4: E.C.3.4.22.69 - Sars coronavirus main proteinase.

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

Added reference

J Mol Biol 402:619-628 (2010)

PubMed id: 20709084

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

M.A.Johnson, K.Jaudzems, K.Wüthrich.

ABSTRACT

The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.