| Literature DB >> 22078568 |
Leidamarie Tirado-Lee1, Allen Lee, Douglas C Rees, Heather W Pinkett.
Abstract
molA (HI1472) from H. influenzae encodes a periplasmic binding protein (PBP) that delivers substrate to the ABC transporter MolB(2)C(2) (formerly HI1470/71). The structures of MolA with molybdate and tungstate in the binding pocket were solved to 1.6 and 1.7 Å resolution, respectively. The MolA-binding protein binds molybdate and tungstate, but not other oxyanions such as sulfate and phosphate, making it the first class III molybdate-binding protein structurally solved. The ∼100 μM binding affinity for tungstate and molybdate is significantly lower than observed for the class II ModA molybdate-binding proteins that have nanomolar to low micromolar affinity for molybdate. The presence of two molybdate loci in H. influenzae suggests multiple transport systems for one substrate, with molABC constituting a low-affinity molybdate locus. Copyright ÂEntities:
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Year: 2011 PMID: 22078568 PMCID: PMC3258573 DOI: 10.1016/j.str.2011.10.004
Source DB: PubMed Journal: Structure ISSN: 0969-2126 Impact factor: 5.006