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Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation.

Publication ,  Journal Article
Rudolph, MJ; Wuebbens, MM; Rajagopalan, KV; Schindelin, H
Published in: Nat Struct Biol
January 2001

Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes, including humans. Genetic deficiencies of enzymes involved in Moco biosynthesis in humans lead to a severe and usually fatal disease. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of MPT is generated by MPT synthase, which consists of a large and small subunits. The 1.45 A resolution crystal structure of MPT synthase reveals a heterotetrameric protein in which the C-terminus of each small subunit is inserted into a large subunit to form the active site. In the activated form of the enzyme this C-terminus is present as a thiocarboxylate. In the structure of a covalent complex of MPT synthase, an isopeptide bond is present between the C-terminus of the small subunit and a Lys side chain in the large subunit. The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway.

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Published In

Nat Struct Biol

DOI

ISSN

1072-8368

Publication Date

January 2001

Volume

8

Issue

1

Start / End Page

42 / 46

Location

United States

Related Subject Headings

  • Ubiquitins
  • Sulfurtransferases
  • Structure-Activity Relationship
  • Static Electricity
  • Sequence Alignment
  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Molecular Sequence Data
  • Models, Molecular
  • Mass Spectrometry
 

Citation

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Rudolph, M. J., Wuebbens, M. M., Rajagopalan, K. V., & Schindelin, H. (2001). Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol, 8(1), 42–46. https://doi.org/10.1038/83034
Rudolph, M. J., M. M. Wuebbens, K. V. Rajagopalan, and H. Schindelin. “Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation.Nat Struct Biol 8, no. 1 (January 2001): 42–46. https://doi.org/10.1038/83034.
Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol. 2001 Jan;8(1):42–6.
Rudolph, M. J., et al. “Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation.Nat Struct Biol, vol. 8, no. 1, Jan. 2001, pp. 42–46. Pubmed, doi:10.1038/83034.
Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol. 2001 Jan;8(1):42–46.

Published In

Nat Struct Biol

DOI

ISSN

1072-8368

Publication Date

January 2001

Volume

8

Issue

1

Start / End Page

42 / 46

Location

United States

Related Subject Headings

  • Ubiquitins
  • Sulfurtransferases
  • Structure-Activity Relationship
  • Static Electricity
  • Sequence Alignment
  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Molecular Sequence Data
  • Models, Molecular
  • Mass Spectrometry