PROSITE documentation PDOC51866Mop domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Schuettelkopf A.W. Harrison J.A. Boxer D.H. Hunter W.N. |
| Title | Passive acquisition of ligand by the MopII molbindin from Clostridium pasteurianum: structures of apo and oxyanion-bound forms. | |
| Source | J. Biol. Chem. 277:15013-15020(2002). | |
| PubMed ID | 11836258 | |
| DOI | 10.1074/jbc.M201005200 |
| 2 | Authors | Delarbre L. Stevenson C.E.M. White D.J. Mitchenall L.A. Pau R.N. Lawson D.M. |
| Title | Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity. | |
| Source | J. Mol. Biol. 308:1063-1079(2001). | |
| PubMed ID | 11352591 | |
| DOI | 10.1006/jmbi.2001.4636 |
| 3 | Authors | Gerber S. Comellas-Bigler M. Goetz B.A. Locher K.P. |
| Title | Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. | |
| Source | Science 321:246-250(2008). | |
| PubMed ID | 18511655 | |
| DOI | 10.1126/science.1156213 |
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