Literature summary for 3.4.21.53 extracted from

Kereiche, S.; Kovacik, L.; Bednar, J.; Pevala, V.; Kunova, N.; Ondrovicova, G.; Bauer, J.; Ambro, L.; Bellova, J.; Kutejova, E.; Raska, I.
The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease (2016), Sci. Rep., 6, 33631 .

Search for more literature for 3.4.21.53

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	binding of protein substrates by Lon stimulates its ATPase and peptidase activities and that this activation is likely to be allosteric	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
gene Lonp1	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme mutant S855A in complex with non-hydrolyzable ATP analogue AMP-PNP and with ADP, X-ray diffraction structure determination and analysis at resolutions of 15 A and 21 A, respectively, fitting of X-rays structures and cryo-electron microscopy structures, overview	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a hLon mutant lacking the first 156 amino acids, the mutant's enzymatic activities and its 3D structure are severely disturbed	Homo sapiens
S855A	site-directed mutagenesis, a proteolytically inactive hLon mutant which retains near wild-type levels of ATPase activity	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
ADP	-	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	mitochondrial Lon protease contains a mitochondrial targeting sequence	Homo sapiens	5739	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P36776	-	-

Subunits

Subunits	Comment	Organism
hexamer	hLon has a unique three-dimensional structure, in which the proteolytic and ATP-binding domains (AP-domain) form a hexameric chamber, while the N-terminal domain is arranged as a trimer of dimers. These two domains are linked by a narrow trimeric channel composed likely of coiled-coil helices. In the presence of AMP-PNP, the AP-domain has a closedring conformation and its N-terminal entry gate appears closed, but in ADP binding, it switches to a lock-washer conformation and its N-terminal gate opens, which is accompanied by a rearrangement of the N-terminal domain. hLon's N-terminal domains are crucial for the overall structure of the hLon, maintaining a conformation allowing its proper functioning. Domain structure, overview	Homo sapiens
More	model on the quaternary structure of the full-length enzyme protein	Homo sapiens

Synonyms

Synonyms	Comment	Organism
hLon	-	Homo sapiens
LONP1	-	Homo sapiens
mitochondrial Lon protease	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	conformational changes are induced by ATP binding and hydrolysis	Homo sapiens

General Information

General Information	Comment	Organism
evolution	human Lon (hLon) is a mitochondrial AAA+ protein (ATPases associated with diverse cellular activities) belonging to the LonA protease subfamily	Homo sapiens
malfunction	altered expression levels of the human mitochondrial Lon protease (hLon) are linked to serious diseases including myopathies, paraplegia, and cancer. The enzymatic activities and the 3D structure of a hLon mutant lacking the first 156 amino acids are severely disturbed	Homo sapiens
additional information	hLon's N-terminal domains are crucial for the overall structure of the hLon, maintaining a conformation allowing its proper functioning. Model on the quaternary structure of the full-length enzyme protein	Homo sapiens
physiological function	Lon is an essential, multitasking AAA+ protease regulating many cellular processes in species across all kingdoms of life. It plays crucial role in the maintenance of mitochondrial homeostasis. Structure-based regulation of Lon enzyme function, overview	Homo sapiens

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Release 2023.1 (January 2023)