Sandbox Reserved 1644: Difference between revisions
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<p align="justify">'''2x36''' is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This domain belongs to the [https://en.wikipedia.org/wiki/Lon_protease_family Lon protease family]. | <p align="justify">'''2x36''' is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This domain belongs to the [https://en.wikipedia.org/wiki/Lon_protease_family Lon protease family]. | ||
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[https://en.wikipedia.org/wiki/Mitochondrion Mitochondrial] Lon [https://en.wikipedia.org/wiki/Protease protease] is an '''ATP-dependent serine protease''' involved in the selective degradation of abnormal proteins. [https://en.wikipedia.org/wiki/LONP1 LONP1] situated on chromosome 19 is the nuclear gene encoding mitochondrial Lon protein. The single species of [https://en.wikipedia.org/wiki/Messenger_RNA mRNA] of this protein is found in the mitochondrial matrix. This protein from human tissues has a molecular mass of 100 [https://en.wikipedia.org/wiki/Dalton_(unit) kDA]. | [https://en.wikipedia.org/wiki/Mitochondrion Mitochondrial] Lon [https://en.wikipedia.org/wiki/Protease protease] is an '''ATP-dependent serine protease''' involved in the selective degradation of abnormal proteins. [https://en.wikipedia.org/wiki/LONP1 LONP1] situated on chromosome 19 is the nuclear gene encoding mitochondrial Lon protein. The single species of [https://en.wikipedia.org/wiki/Messenger_RNA mRNA] of this protein is found in the mitochondrial matrix. This protein from human tissues has a molecular mass of 100 [https://en.wikipedia.org/wiki/Dalton_(unit) kDA].</p> | ||
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== Function == | == Function == | ||
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Mitochondrial Lon protease interacts with [https://en.wikipedia.org/wiki/Chaperone_(protein) protein chaperone], notably [https://en.wikipedia.org/wiki/Chaperonin HSP60]-[https://en.wikipedia.org/wiki/Hsp70 Hsp70] complex to protect cell from apoptosis under environmental stress<ref>Bota, Daniela A., and Kelvin J. A. Davies. “Mitochondrial Lon Protease in Human Disease and Aging: Including an Etiologic Classification of Lon-Related Diseases and Disorders.” Free Radical Biology & Medicine 100 (November 2016): 188–98. https://doi.org/10.1016/j.freeradbiomed.2016.06.031.</ref>. | Mitochondrial Lon protease interacts with [https://en.wikipedia.org/wiki/Chaperone_(protein) protein chaperone], notably [https://en.wikipedia.org/wiki/Chaperonin HSP60]-[https://en.wikipedia.org/wiki/Hsp70 Hsp70] complex to protect cell from apoptosis under environmental stress<ref>Bota, Daniela A., and Kelvin J. A. Davies. “Mitochondrial Lon Protease in Human Disease and Aging: Including an Etiologic Classification of Lon-Related Diseases and Disorders.” Free Radical Biology & Medicine 100 (November 2016): 188–98. https://doi.org/10.1016/j.freeradbiomed.2016.06.031.</ref>. | ||
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The mitochondrial Lon protease is essentially found in the cytoplasmic of mitochondria because [https://en.wikipedia.org/wiki/Amino_acid amino-acid] has a potential mitochondrial targetting presequences<ref>García-Nafría, Javier, Gabriela Ondrovičová, Elena Blagova, Vladimir M Levdikov, Jacob A Bauer, Carolyn K Suzuki, Eva Kutejová, Anthony J Wilkinson, and Keith S Wilson. “Structure of the Catalytic Domain of the Human Mitochondrial Lon Protease: Proposed Relation of Oligomer Formation and Activity.” Protein Science : A Publication of the Protein Society 19, no. 5 (May 2010): 987–99. https://doi.org/10.1002/pro.376.</ref>. | The mitochondrial Lon protease is essentially found in the cytoplasmic of mitochondria because [https://en.wikipedia.org/wiki/Amino_acid amino-acid] has a potential mitochondrial targetting presequences<ref>García-Nafría, Javier, Gabriela Ondrovičová, Elena Blagova, Vladimir M Levdikov, Jacob A Bauer, Carolyn K Suzuki, Eva Kutejová, Anthony J Wilkinson, and Keith S Wilson. “Structure of the Catalytic Domain of the Human Mitochondrial Lon Protease: Proposed Relation of Oligomer Formation and Activity.” Protein Science : A Publication of the Protein Society 19, no. 5 (May 2010): 987–99. https://doi.org/10.1002/pro.376.</ref>.</p> | ||
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== General structure == | == General structure == | ||
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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 [https://en.wikipedia.org/wiki/Alternative_splicing alternative splicing] of the portion of DNA coding for this protein. | <p align="justify">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 [https://en.wikipedia.org/wiki/Alternative_splicing 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. | 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 [https://en.wikipedia.org/wiki/Protease protease] complex. (This structure is similar with yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] ) | Lon proteins are therefore an hexameric chambered [https://en.wikipedia.org/wiki/Protease protease] complex. (This structure is similar with yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] ) | ||
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This protein has a [https://en.wikipedia.org/wiki/Proteolysis '''proteolytic'''] and [https://en.wikipedia.org/wiki/Chaperone_(protein) '''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. | This protein has a [https://en.wikipedia.org/wiki/Proteolysis '''proteolytic'''] and [https://en.wikipedia.org/wiki/Chaperone_(protein) '''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. | ||
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The Lon protein has three main distinct domains: the first, the '''N-terminal''' domain, is specialised in '''substrate binding''' and [https://en.wikipedia.org/wiki/Oligomer '''oligomerization''']. The second, called the '''AAA+ domain''' (or A domain) corresponds to the fixation and hydrolysis site of the [https://biologydictionary.net/atp/ATP ATP]. Finally, the third domain located at the '''C-terminal''' is an active serine site leading to '''substrate degradation'''. This is a [https://en.wikipedia.org/wiki/Proteolysis '''proteolytic'''] domain, called domain P. | The Lon protein has three main distinct domains: the first, the '''N-terminal''' domain, is specialised in '''substrate binding''' and [https://en.wikipedia.org/wiki/Oligomer '''oligomerization''']. The second, called the '''AAA+ domain''' (or A domain) corresponds to the fixation and hydrolysis site of the [https://biologydictionary.net/atp/ATP ATP]. Finally, the third domain located at the '''C-terminal''' is an active serine site leading to '''substrate degradation'''. This is a [https://en.wikipedia.org/wiki/Proteolysis '''proteolytic'''] domain, called domain P.</p> | ||
