Unknown

Dataset Information

0

Crystal structure of the moloney murine leukemia virus RNase H domain.


ABSTRACT: A crystallographic study of the Moloney murine leukemia virus (Mo-MLV) RNase H domain was performed to provide information about its structure and mechanism of action. These efforts resulted in the crystallization of a mutant Mo-MLV RNase H lacking the putative helix C (DeltaC). The 1.6-Angstroms resolution structure resembles the known structures of the human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H. The structure revealed the coordination of a magnesium ion within the catalytic core comprised of the highly conserved acidic residues D524, E562, and D583. Surface charge mapping of the Mo-MLV structure revealed a high density of basic charges on one side of the enzyme. Using a model of the Mo-MLV structure superimposed upon a structure of HIV-1 reverse transcriptase bound to an RNA/DNA hybrid substrate, Mo-MLV RNase H secondary structures and individual amino acids were examined for their potential roles in binding substrate. Identified regions included Mo-MLV RNase H beta1-beta2, alphaA, and alphaB and residues from alphaB to alphaD and its following loop. Most of the identified substrate-binding residues corresponded with residues directly binding nucleotides in an RNase H from Bacillus halodurans as observed in a cocrystal structure with RNA/DNA. Finally, superimposition of RNases H of Mo-MLV, E. coli, and HIV-1 revealed that a loop of the HIV-1 connection domain resides within the same region of the Mo-MLV and E. coli C-helix. The HIV-1 connection domain may serve to recognize and bind the RNA/DNA substrate major groove.

SUBMITTER: Lim D 

PROVIDER: S-EPMC1563865 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystal structure of the moloney murine leukemia virus RNase H domain.

Lim David D   Gregorio G Glenn GG   Bingman Craig C   Martinez-Hackert Erik E   Hendrickson Wayne A WA   Goff Stephen P SP  

Journal of virology 20060901 17


A crystallographic study of the Moloney murine leukemia virus (Mo-MLV) RNase H domain was performed to provide information about its structure and mechanism of action. These efforts resulted in the crystallization of a mutant Mo-MLV RNase H lacking the putative helix C (DeltaC). The 1.6-Angstroms resolution structure resembles the known structures of the human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H. The structure revealed the coordination of a magnesium ion within the  ...[more]

Similar Datasets

| S-EPMC2798349 | biostudies-literature
| S-EPMC1636480 | biostudies-literature
| S-EPMC4000802 | biostudies-literature
| S-EPMC5357174 | biostudies-literature
| S-EPMC1462987 | biostudies-literature
| S-EPMC3423011 | biostudies-literature
| S-EPMC2798346 | biostudies-literature
| S-EPMC112395 | biostudies-literature
| S-EPMC533042 | biostudies-literature
| S-EPMC4917968 | biostudies-literature