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Structure. 2011 Nov 9;19(11):1701-10. doi: 10.1016/j.str.2011.10.004.

Classification of a Haemophilus influenzae ABC transporter HI1470/71 through its cognate molybdate periplasmic binding protein, MolA.

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1
Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.

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.

PMID:
22078568
PMCID:
PMC3258573
DOI:
10.1016/j.str.2011.10.004
[Indexed for MEDLINE]
Free PMC Article
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