From Proteopedia
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| - | [[Image:1cu1.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1cu1| PDB=1cu1 | SCENE= }} | | {{STRUCTURE_1cu1| PDB=1cu1 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF AN ENZYME COMPLEX FROM HEPATITIS C VIRUS'''
| + | ===CRYSTAL STRUCTURE OF AN ENZYME COMPLEX FROM HEPATITIS C VIRUS=== |
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| - | ==Overview==
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| - | BACKGROUND: Hepatitis C virus (HCV) currently infects approximately 3% of the world's population. HCV RNA is translated into a polyprotein that during maturation is cleaved into functional components. One component, nonstructural protein 3 (NS3), is a 631-residue bifunctional enzyme with protease and helicase activities. The NS3 serine protease processes the HCV polyprotein by both cis and trans mechanisms. The structural aspects of cis processing, the autoproteolysis step whereby the protease releases itself from the polyprotein, have not been characterized. The structural basis for inclusion of protease and helicase activities in a single polypeptide is also unknown. RESULTS: We report here the 2.5 A resolution structure of an engineered molecule containing the complete NS3 sequence and the protease activation domain of nonstructural protein 4A (NS4A) in a single polypeptide chain (single chain or scNS3-NS4A). In the molecule, the helicase and protease domains are segregated and connected by a single strand. The helicase necleoside triphosphate and RNA interaction sites are exposed to solvent. The protease active site of scNS3-NS4A is occupied by the NS3 C terminus, which is part of the helicase domain. Thus, the intramolecular complex shows one product of NS3-mediated cleavage at the NS3-NS4A junction of the HCV polyprotein bound at the protease active site. CONCLUSIONS: The scNS3-NS4A structure provides the first atomic view of polyprotein cis processing. Both local and global structural rearrangements follow the cis cleavage reaction, and large segments of the polyprotein can be folded prior to proteolytic processing. That the product complex of the cis cleavage reaction exists in a stable molecular conformation suggests autoinhibition and substrate-induced activation mechanisms for regulation of NS3 protease activity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10574797}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10574797 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10574797}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Bifunctional,protease-helicase]] | | [[Category: Bifunctional,protease-helicase]] |
| | [[Category: Hepatitis c virus]] | | [[Category: Hepatitis c virus]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:06:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:22:12 2008'' |
Revision as of 18:22, 30 June 2008
Template:STRUCTURE 1cu1
CRYSTAL STRUCTURE OF AN ENZYME COMPLEX FROM HEPATITIS C VIRUS
Template:ABSTRACT PUBMED 10574797
About this Structure
1CU1 is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.
Reference
Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase., Yao N, Reichert P, Taremi SS, Prosise WW, Weber PC, Structure. 1999 Nov 15;7(11):1353-63. PMID:10574797
Page seeded by OCA on Mon Jun 30 21:22:12 2008
