{PDOC51866}
{PS51866; MOP}
{BEGIN}
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* Mop domain profile *
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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 beta-strands linked by
short loops.  It  contains  a beta-barrel comprised of five antiparallel beta-
strands in  a  Greek  key  arrangement that is capped by amphipathic two-turns
alpha-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 2018 / First entry.

[ 1] Schuettelkopf A.W., Harrison J.A., Boxer D.H., Hunter W.N.
     "Passive acquisition of ligand by the MopII molbindin from Clostridium
     pasteurianum: structures of apo and oxyanion-bound forms."
     J. Biol. Chem. 277:15013-15020(2002).
     PubMed=11836258; DOI=10.1074/jbc.M201005200
[ 2] Delarbre L., Stevenson C.E.M., White D.J., Mitchenall L.A., Pau R.N.,
     Lawson D.M.
     "Two crystal structures of the cytoplasmic molybdate-binding protein
     ModG suggest  a novel cooperative binding mechanism and provide
     insights into ligand-binding specificity."
     J. Mol. Biol. 308:1063-1079(2001).
     PubMed=11352591; DOI=10.1006/jmbi.2001.4636
[ 3] Gerber S., Comellas-Bigler M., Goetz B.A., Locher K.P.
     "Structural basis of trans-inhibition in a molybdate/tungstate ABC
     transporter."
     Science 321:246-250(2008).
     PubMed=18511655; DOI=10.1126/science.1156213

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