Single-domain HEPN
proteins found in many bacteria.
Two-domain
proteins with N-terminal
nucleotidyltransferase (NT) and C- terminal HEPN
domains. This N-terminal NT domain belongs to a large family of NTs, which includes several classes of
enzymes that are responsible for some types of
bacterial resistance to
aminoglycosides. These enzymes deactivate various
antibiotics by transferring a
nucleotidyl group to the drug.
A multidomain sacsin protein in
genomes of
fish and
mammals. The HEPN domain is located at the C terminus of the protein, directly after the DnaJ domain. The
crystal structure of the HEPN domain from the TM0613 protein of Thermotoga maritima indicates that it is
structurally similar to the C-terminal all-
alpha-helical domain of
kanamycin nucleotidyltransferases (KNTases). It is composed of five alpha helices, three of which form an up- and-down helical bundle, with a pair of short
helices on the side. The distant structural similarity suggests that the HEPN domain might be involved in nucleotide binding.[1]
References
^Grynberg M, Erlandsen H, Godzik A (May 2003). "HEPN: a common domain in bacterial drug resistance and human neurodegenerative proteins". Trends Biochem. Sci. 28 (5): 224–6.
doi:
10.1016/S0968-0004(03)00060-4.
PMID12765831.
Single-domain HEPN
proteins found in many bacteria.
Two-domain
proteins with N-terminal
nucleotidyltransferase (NT) and C- terminal HEPN
domains. This N-terminal NT domain belongs to a large family of NTs, which includes several classes of
enzymes that are responsible for some types of
bacterial resistance to
aminoglycosides. These enzymes deactivate various
antibiotics by transferring a
nucleotidyl group to the drug.
A multidomain sacsin protein in
genomes of
fish and
mammals. The HEPN domain is located at the C terminus of the protein, directly after the DnaJ domain. The
crystal structure of the HEPN domain from the TM0613 protein of Thermotoga maritima indicates that it is
structurally similar to the C-terminal all-
alpha-helical domain of
kanamycin nucleotidyltransferases (KNTases). It is composed of five alpha helices, three of which form an up- and-down helical bundle, with a pair of short
helices on the side. The distant structural similarity suggests that the HEPN domain might be involved in nucleotide binding.[1]
References
^Grynberg M, Erlandsen H, Godzik A (May 2003). "HEPN: a common domain in bacterial drug resistance and human neurodegenerative proteins". Trends Biochem. Sci. 28 (5): 224–6.
doi:
10.1016/S0968-0004(03)00060-4.
PMID12765831.