1c0m
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
- | |ACTIVITY= [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c0m OCA], [http://www.ebi.ac.uk/pdbsum/1c0m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c0m RCSB]</span> | ||
}} | }} | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:12:08 2008'' |
Revision as of 16:12, 30 March 2008
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, resolution 2.53Å | |||||||
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Activity: | RNA-directed DNA polymerase, with EC number 2.7.7.49 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF RSV TWO-DOMAIN INTEGRASE
Overview
Integration of retroviral cDNA is a necessary step in viral replication. The virally encoded integrase protein and DNA sequences at the ends of the linear viral cDNA are required for this reaction. Previous studies revealed that truncated forms of Rous sarcoma virus integrase containing two of the three protein domains can carry out integration reactions in vitro. Here, we describe the crystal structure at 2.5 A resolution of a fragment of the integrase of Rous sarcoma virus (residues 49-286) containing both the conserved catalytic domain and a modulatory DNA-binding domain (C domain). The catalytic domains form a symmetric dimer, but the C domains associate asymmetrically with each other and together adopt a canted conformation relative to the catalytic domains. A binding path for the viral cDNA is evident spanning both domain surfaces, allowing modeling of the larger integration complexes that are known to be active in vivo. The modeling suggests that formation of an integrase tetramer (a dimer of dimers) is necessary and sufficient for joining both viral cDNA ends at neighboring sites in the target DNA. The observed asymmetric arrangement of C domains suggests that they could form a rotationally symmetric tetramer that may be important for bridging integrase complexes at each cDNA end.
About this Structure
1C0M is a Single protein structure of sequence from Rous sarcoma virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of an active two-domain derivative of Rous sarcoma virus integrase., Yang ZN, Mueser TC, Bushman FD, Hyde CC, J Mol Biol. 2000 Feb 18;296(2):535-48. PMID:10669607
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