Document Detail


Retroviral integrase superfamily: the structural perspective.
MedLine Citation:
PMID:  19165139     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The retroviral integrase superfamily (RISF) comprises numerous important nucleic acid-processing enzymes, including transposases, integrases and various nucleases. These enzymes are involved in a wide range of processes such as transposition, replication and repair of DNA, homologous recombination, and RNA-mediated gene silencing. Two out of the four enzymes that are encoded by the human immunodeficiency virus--RNase H1 and integrase--are members of this superfamily. RISF enzymes act on various substrates, and yet show remarkable mechanistic and structural similarities. All share a common fold of the catalytic core and the active site, which is composed primarily of carboxylate residues. Here, I present RISF proteins from a structural perspective, describing the individual members and the common and divergent elements of their structures, as well as the mechanistic insights gained from the structures of RNase H1 enzyme complexes with RNA/DNA hybrids.
Authors:
Marcin Nowotny
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2009-01-23
Journal Detail:
Title:  EMBO reports     Volume:  10     ISSN:  1469-3178     ISO Abbreviation:  EMBO Rep.     Publication Date:  2009 Feb 
Date Detail:
Created Date:  2009-02-02     Completed Date:  2009-03-16     Revised Date:  2013-06-02    
Medline Journal Info:
Nlm Unique ID:  100963049     Medline TA:  EMBO Rep     Country:  England    
Other Details:
Languages:  eng     Pagination:  144-51     Citation Subset:  IM    
Affiliation:
Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, 4 Ks. Trojdena Street, 02-109, Warsaw, Poland. mnowotny@iimcb.gov.pl
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MeSH Terms
Descriptor/Qualifier:
Animals
Bacterial Proteins / chemistry,  physiology
Catalytic Domain
Dimerization
Hydrolysis
Integrases / chemistry*,  physiology
Mammals / metabolism
Mice
Models, Molecular
Multigene Family*
Nucleic Acids / metabolism
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Retroviridae Proteins / chemistry*,  physiology
Ribonuclease H / chemistry,  physiology
Species Specificity
Structure-Activity Relationship
Substrate Specificity
Transposases / chemistry,  physiology
Viral Proteins / chemistry,  physiology
Grant Support
ID/Acronym/Agency:
081760//Wellcome Trust; //Wellcome Trust
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Nucleic Acids; 0/Retroviridae Proteins; 0/Viral Proteins; EC 2.7.7.-/Integrases; EC 2.7.7.-/Transposases; EC 3.1.26.4/Ribonuclease H; EC 3.1.26.4/ribonuclease HI
Comments/Corrections

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