G3DSA:2.40.340.10

MoeA, C-terminal, domain IV

CATH-Gene3D entry
Member databaseCATH-Gene3D
CATH-Gene3D typehomologous superfamily

Description
Imported from IPR036688

The majority of molybdenum-containing enzymes utilise a molybdenum cofactor (MoCF or Moco) consisting of a Mo atom coordinated via a cis-dithiolene moiety to molybdopterin (MPT). MoCF is ubiquitous in nature, and the pathway for MoCF biosynthesis is conserved in all three domains of life. MoCF-containing enzymes function as oxidoreductases in carbon, nitrogen, and sulphur metabolism
[2, 3]
.

This domain is found in proteins involved in biosynthesis of molybdopterin cofactor however the exact molecular function of this domain is uncertain. The structure of this domain is known
[1]
and forms an incomplete β barrel.

References
Imported from IPR036688

1.The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Xiang S, Nichols J, Rajagopalan KV, Schindelin H. Structure 9, 299-310, (2001). View articlePMID: 11525167

2.Cell biology of molybdenum. Mendel RR, Bittner F. Biochim. Biophys. Acta 1763, 621-35, (2006). View articlePMID: 16784786

3.Molybdenum and tungsten in biology. Hille R. Trends Biochem. Sci. 27, 360-7, (2002). View articlePMID: 12114025

Further reading

4. Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three Escherichia coli proteins. Stallmeyer B, Nerlich A, Schiemann J, Brinkmann H, Mendel RR. Plant J. 8, 751-62, (1995). View articlePMID: 8528286

5. Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft. Nichols JD, Xiang S, Schindelin H, Rajagopalan KV. Biochemistry 46, 78-86, (2007). View articlePMID: 17198377

6. In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli. Magalon A, Frixon C, Pommier J, Giordano G, Blasco F. J. Biol. Chem. 277, 48199-204, (2002). View articlePMID: 12372836

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