Structures from the SARS-CoV proteomics project
Peter Kuhn group (The Scripps Research Institute) and collaborators
Peter Kuhn's group from The Scripps Research Institute has
provided several examples of structures determined from the SARS-CoV
proteomics project using data from GM/CA-CAT (as well as from SSRL) . These
three structures include two important non-structural proteins, nsp10 and
nsp15, and the third was an RNA-binding domain of the SARS nucleocapsid. The
2.9-Å Nsp15 structure of a deletion construct truncated at both the C-
and N- terminus required extensive screening of multiple protein constructs.
This structure revealed that truncation of the N-terminal oligomerization
domains turns it from a hexameric endonuclease into an obligate monomer which
is inactive. The primary reason for the loss of catalytic activity was found
to be a dramatic collapse of the two active site loops that support the
nucleotide ligand and metal ion during catalysis.
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Figure: Structure of an N-Terminal
Truncated Form of Nendou (NSP15) From SARS-CORONAVIRUS [PDB ID
2OZK] |
Citation:
| [1] |
Joseph, JS, Saikatendu, KS, Subramanian, V, Neuman, BW, Brooun, A, Griffith,
M, Moy, K, Yadav, MK, Velasquez, J, Buchmeier, MJ, Stevens, RC, Kuhn, P.
Crystal Structure of Nonstructural Protein 10 from the Severe Acute
Respiratory Syndrome Coronavirus Reveals a Novel Fold with Two Zinc-Binding
Motifs, J. Virol. 80 (16), 7894-7901 (2006). DOI: 10.1128/JVI.00467-06. |
| [2] |
Joseph, JS, Saikatendu, KS, Subramanian, V, Neuman, BW, Buchmeier, MJ,
Stevens, RC, Kuhn, P. Crystal Structure of a Monomeric Form of Severe Acute
Respiratory Syndrome Coronavirus Endonuclease nsp15 Suggests a Role for
Hexamerization as an Allosteric Switch, J. Virol. 81 (12), 6700-6708 (2007).
DOI: 10.1128/JVI.02817-06. |
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