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PROSITE documentation PDOC51866 [for PROSITE entry PS51866]

Mop domain profile





Description

Mop domains, which occur in a variety of bacterial and archeal proteins specifically bind molybdate (or tungstate). The simplest mop-containing proteins are the so-called molbindins, consisting entirely of either one or two mop domains. The physiological role of these proteins is unclear, although they have been implicated in molybdate storage and homeostasis. Other mop-containing proteins are ModC, a component of the high affinity ABC transporter, and ModE, the molybdate-dependent transcriptional regulator [1,2,3].

The mop domain of 68 amino acid residues contains six β-strands linked by short loops. It contains a β-barrel comprised of five antiparallel β-strands in a Greek key arrangement that is capped by amphipathic two-turns α-helices (see <PDB:1H9J>). The Mop domain structure corresponds to the canonical oligonucleotide/oligosaccharide binding (OB) fold [1,2,3].

The profile we developed covers the entire mop domain.

Last update:

July 2018 / First entry.

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Technical section

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

MOP, PS51866; Mop domain profile  (MATRIX)


References

1AuthorsSchuettelkopf A.W. Harrison J.A. Boxer D.H. Hunter W.N.
TitlePassive acquisition of ligand by the MopII molbindin from Clostridium pasteurianum: structures of apo and oxyanion-bound forms.
SourceJ. Biol. Chem. 277:15013-15020(2002).
PubMed ID11836258
DOI10.1074/jbc.M201005200

2AuthorsDelarbre L. Stevenson C.E.M. White D.J. Mitchenall L.A. Pau R.N. Lawson D.M.
TitleTwo crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity.
SourceJ. Mol. Biol. 308:1063-1079(2001).
PubMed ID11352591
DOI10.1006/jmbi.2001.4636

3AuthorsGerber S. Comellas-Bigler M. Goetz B.A. Locher K.P.
TitleStructural basis of trans-inhibition in a molybdate/tungstate ABC transporter.
SourceScience 321:246-250(2008).
PubMed ID18511655
DOI10.1126/science.1156213



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