1sh2
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(New page: 200px<br /><applet load="1sh2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sh2, resolution 2.30Å" /> '''Crystal Structure of...)
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Revision as of 22:21, 24 November 2007
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Crystal Structure of Norwalk Virus Polymerase (Metal-free, Centered Orthorhombic)
Overview
Norwalk virus is a major cause of acute gastroenteritis for which, effective treatments are sorely lacking. To provide a basis for the, rational design of novel antiviral agents, the main replication enzyme in, Norwalk virus, the virally encoded RNA-dependent RNA polymerase (RdRP), has been expressed in an enzymatically active form, and its structure has, been crystallographically determined both in the presence and absence of, divalent metal cations. Although the overall fold of the enzyme is similar, to that seen previously in the RdRP from rabbit hemorrhagic disease virus, the carboxyl terminus, surprisingly, is located in the active site cleft, in five independent copies of the protein in three distinct crystal forms., The location of this carboxyl-terminal segment appears to interfere with, the binding of double-stranded RNA in the active site cleft and may play a, role in the initiation of RNA synthesis or mediate interactions with, accessory replication proteins.
About this Structure
1SH2 is a Single protein structure of sequence from Norwalk virus. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft., Ng KK, Pendas-Franco N, Rojo J, Boga JA, Machin A, Alonso JM, Parra F, J Biol Chem. 2004 Apr 16;279(16):16638-45. Epub 2004 Feb 5. PMID:14764591
Page seeded by OCA on Sun Nov 25 00:28:59 2007
