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PROSITE documentation PDOC51787 [for PROSITE entry PS51787]

Lon N-terminal domain profile





Description

Lon (also known as endopeptidase La, EC 3.4.21.53) is a multi-domain ATP-dependent protease found throughout all kingdoms of life. It is involved in protein quality control and several regulatory processes. All Lon proteases contain an ATPase domain belonging to the AAA+ superfamily of molecular machines, and a proteolytic domain (see <PDOC51786>) with a serine-lysine catalytic dyad in which a lysine assists the catalytic serine in proteolytic cleavage. Lon proteases can be divided into two subfamilies: A type (A-Lons), which have a large multi-lobed N-terminal domain together with the ATPase and protease domains, and B type (B-Lons), which lack an N domain, but have a membrane-anchoring region emerging from the ATPase domain. B-Lons are found in Archaea, in which they are the lone membrane-anchored ATP-dependent protease. The soluble A-Lons are found in all bacteria and in eukaryotic cell organelles, such as mitochondria and peroxisomes, and are needed for recovery from various stress conditions [1,2,3,4,5,6]. Animal cereblon (CRBN) is a ubiquitously expressed protein that is part of the cullin-4-containing E3 ubiquitin ligase complex CUL4-RBX1-DDB1 (known as CRL4). It contain an N-terminal domain that ressembles the one of A-Lons [7]. The Lon N-terminal domain is thought to be involved in substrate binding and might represent a general protein and polypeptide interaction domain [1,2].

The structure of the Lon N-terminal domain consists of two distinct regions, connected by an extended loop: a compact β-sheet rich, globular subdomain, and an additional α-helical subdomain (see <PDB:3M65>) [1,2].

The profile we developed covers the entire Lon N-terminal domain.

Last update:

January 2016 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

LON_N, PS51787; Lon N-terminal domain profile  (MATRIX)


References

1AuthorsDuman R.E. Loewe J.
TitleCrystal structures of Bacillus subtilis Lon protease.
SourceJ. Mol. Biol. 401:653-670(2010).
PubMed ID20600124
DOI10.1016/j.jmb.2010.06.030

2AuthorsLi M. Rasulova F. Melnikov E.E. Rotanova T.V. Gustchina A. Maurizi M.R. Wlodawer A.
TitleCrystal structure of the N-terminal domain of E. coli Lon protease.
SourceProtein Sci. 14:2895-2900(2005).
PubMed ID16199667
DOI10.1110/ps.051736805

3AuthorsBotos I. Melnikov E.E. Cherry S. Kozlov S. Makhovskaya O.V. Tropea J.E. Gustchina A. Rotanova T.V. Wlodawer A.
TitleAtomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases.
SourceJ. Mol. Biol. 351:144-157(2005).

4AuthorsRotanova T.V. Botos I. Melnikov E.E. Rasulova F. Gustchina A. Maurizi M.R. Wlodawer A.
TitleSlicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
SourceProtein Sci. 15:1815-1828(2006).
PubMed ID16877706
DOI10.1110/ps.052069306

5AuthorsCha S.-S. An Y.J. Lee C.R. Lee H.S. Kim Y.-G. Kim S.J. Kwon K.K. De Donatis G.M. Lee J.-H. Maurizi M.R. Kang S.G.
TitleCrystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.
SourceEMBO J. 29:3520-3530(2010).
PubMed ID20834233
DOI10.1038/emboj.2010.226

6AuthorsGarcia-Nafria J. Ondrovicova G. Blagova E. Levdikov V.M. Bauer J.A. Suzuki C.K. Kutejova E. Wilkinson A.J. Wilson K.S.
TitleStructure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity.
SourceProtein Sci. 19:987-999(2010).
PubMed ID20222013
DOI10.1002/pro.376

7AuthorsFischer E.S. Boehm K. Lydeard J.R. Yang H. Stadler M.B. Cavadini S. Nagel J. Serluca F. Acker V. Lingaraju G.M. Tichkule R.B. Schebesta M. Forrester W.C. Schirle M. Hassiepen U. Ottl J. Hild M. Beckwith R.E.J. Harper J.W. Jenkins J.L. Thomae N.H.
TitleStructure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide.
SourceNature 512:49-53(2014).
PubMed ID25043012
DOI10.1038/nature13527



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