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Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography.

Lakomek K, Dickmanns A, Kettwig M, Urlaub H, Ficner R, Lübke T
BMC Struct Biol 9 56 (2009)
Related entries: 3fbx, 3fgr, 3fgt

Cited: 12 times
EuropePMC logo PMID: 19706171

Abstract

Background

The lysosomal 66.3 kDa protein from mouse is a soluble, mannose 6-phosphate containing protein of so far unknown function. It is synthesized as a glycosylated 75 kDa precursor that undergoes limited proteolysis leading to a 28 kDa N- and a 40 kDa C-terminal fragment.

Results

In order to gain insight into the function and the post-translational maturation process of the glycosylated 66.3 kDa protein, three crystal structures were determined that represent different maturation states. These structures demonstrate that the 28 kDa and 40 kDa fragment which have been derived by a proteolytic cleavage remain associated. Mass spectrometric analysis confirmed the subsequent trimming of the C-terminus of the 28 kDa fragment making a large pocket accessible, at the bottom of which the putative active site is located. The crystal structures reveal a significant similarity of the 66.3 kDa protein to several bacterial hydrolases. The core alphabetabetaalpha sandwich fold and a cysteine residue at the N-terminus of the 40 kDa fragment (C249) classify the 66.3 kDa protein as a member of the structurally defined N-terminal nucleophile (Ntn) hydrolase superfamily.

Articles - 3fgw mentioned but not cited (2)

  1. Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography. Lakomek K, Dickmanns A, Kettwig M, Urlaub H, Ficner R, Lübke T. BMC Struct Biol 9 56 (2009)
  2. p67: a cryptic lysosomal hydrolase in Trypanosoma brucei? Koeller CM, Smith TK, Gulick AM, Bangs JD. Parasitology 148 1271-1276 (2021)


Reviews citing this publication (2)

  1. The proteome of lysosomes. Schröder BA, Wrocklage C, Hasilik A, Saftig P. Proteomics 10 4053-4076 (2010)
  2. The Human Ntn-Hydrolase Superfamily: Structure, Functions and Perspectives. Linhorst A, Lübke T. Cells 11 1592 (2022)

Articles citing this publication (8)

  1. More similar than different: Host cell protein production using three null CHO cell lines. Yuk IH, Nishihara J, Walker D, Huang E, Gunawan F, Subramanian J, Pynn AF, Yu XC, Zhu-Shimoni J, Vanderlaan M, Krawitz DC. Biotechnol Bioeng 112 2068-2083 (2015)
  2. Specific Immune Response to Phospholipase B-Like 2 Protein, a Host Cell Impurity in Lebrikizumab Clinical Material. Fischer SK, Cheu M, Peng K, Lowe J, Araujo J, Murray E, McClintock D, Matthews J, Siguenza P, Song A. AAPS J 19 254-263 (2017)
  3. Molecular mechanism of activation of the immunoregulatory amidase NAAA. Gorelik A, Gebai A, Illes K, Piomelli D, Nagar B. Proc Natl Acad Sci U S A 115 E10032-E10040 (2018)
  4. Structures of an isopenicillin N converting Ntn-hydrolase reveal different catalytic roles for the active site residues of precursor and mature enzyme. Bokhove M, Yoshida H, Hensgens CM, van der Laan JM, Sutherland JD, Dijkstra BW. Structure 18 301-308 (2010)
  5. Characterization of ELISA Antibody-Antigen Interaction using Footprinting-Mass Spectrometry and Negative Staining Transmission Electron Microscopy. Lin M, Krawitz D, Callahan MD, Deperalta G, Wecksler AT. J Am Soc Mass Spectrom 29 961-971 (2018)
  6. The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B. Ullah A, Masood R. Front Mol Biosci 7 175 (2020)
  7. Insights into ultra-low affinity lipase-antibody noncovalent complex binding mechanisms. Hecht ES, Mehta S, Wecksler AT, Aguilar B, Swanson N, Phung W, Dubey Kelsoe A, Benner WH, Tesar D, Kelley RF, Sandoval W, Sreedhara A. MAbs 14 2135183 (2022)
  8. An astonishing wealth of new proteasome homologs. Fuchs ACD, Alva V, Lupas AN. Bioinformatics 37 4694-4703 (2021)


Related citations provided by authors (1)

  1. De novo sulfur SAD phasing of the lysosomal 66.3 kDa protein from mouse.. Lakomek K, Dickmanns A, Mueller U, Kollmann K, Deuschl F, Berndt A, Lübke T, Ficner R Acta Crystallogr D Biol Crystallogr 65 220-8 (2009)

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