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2x36 is a 6 chain structure with sequence from Human. This domain belongs to the Lon protease family.

Mitochondrial Lon protease is an ATP-dependent serine protease involved in the selective degradation of abnormal proteins. LONP1 situated on chromosome 19 is the nuclear gene encoding mitochondrial Lon protein. The single species of mRNA of this protein is found in the mitochondrial matrix. This protein from human tissues has a molecular mass of 100 kDA.

Function

The mitochondrial Lon protease is an important regulator of mitochondrial metabolism including the maintenance and repair of mitochondrial DNA. This protein is also essential for homeostasis of mitochondria, and by regulating some regulatory proteins which have a short life or damaged proteins.

Lon protease has three main roles.

This protein is able to do a proteolytic digestion of oxidized proteins which allows the renewal of essential mitochondrial enzymes such as aconitase or Mitochondrial transcription factor A. Lon protease is involved in mtDNA replication and mitogenesis by being a mitochondrial DNA-bing protein. Mitochondrial Lon protease interacts with protein chaperone, notably HSP60-Hsp70 complex to protect cell from apoptosis under environmental stress^[3].

The mitochondrial Lon protease is essentially found in the cytoplasmic of mitochondria because amino-acid has a potential mitochondrial targetting presequences.

General structure

Lon proteins are grouped into two families, LonA and LonB. The human protein LonP1 is part of the LonA proteins. This protein has three isoforms obtained by alternative splicing of the portion of DNA coding for this protein. Globally there is a great diversity of Lon proteins, but they are all organised in an oligomeric ring structure, mostly hexameric structure with identical subunits. Lon proteins are therefore an hexameric chambered protease complex. (This structure is similar with yeast Pim1 ) The six Lon monomers are forming three pairs of legs owned by the N-terminal domain of the protein. This structure is emerging of the protein as a trimer of dimers.
Like many proteins, Lon is a flexible peptide which has different three-dimensional conformations. The protein can therefore pass from one conformation to another by hydrolysis of ATP. With these conformational changes, the active sites of the Lon protein are protected from the external environment in the oligomeric complex that forms the degradation chamber. This form of degradation chamber is also found in bacteria, plants, fungi and metazoan, the similarities with bacteria are most probably due to the endosymbiotic theory.

This protein has a proteolytic and chaperone-like activity, it cannot unfold aggregated proteins, but can participate in the assembling of some complexes). These two enzymatic activities are separated on two polypeptide chains forming a complex or two separate domains on the same polypeptide chain.
The Lon protein has three main distinct domains: the first, the N-terminal domain, is specialised in substrate binding and oligomerization. The second, called the AAA+ domain (or A domain) corresponds to the fixation and hydrolysis site of the ATP. Finally, the third domain located at the C-terminal is an active serine site leading to substrate degradation. This is a proteolytic domain, called domain P.

Structural highlights

Evolutionary conservation

Disease

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