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Title: Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA

Abstract

molA (HI1472) from H. influenzae encodes a periplasmic binding protein (PBP) that delivers substrate to the ABC transporter MolB{sub 2}C{sub 2} (formerly HI1470/71). The structures of MolA with molybdate and tungstate in the binding pocket were solved to 1.6 and 1.7 {angstrom} 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 {approx}100 {mu}M 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.

Authors:
; ; ;  [1];  [2]
  1. (CIT)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
OTHERNIH
OSTI Identifier:
1034211
Resource Type:
Journal Article
Resource Relation:
Journal Name: Structure; Journal Volume: 19; Journal Issue: (11) ; 11, 2011
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; AFFINITY; CLASSIFICATION; HAEMOPHILUS; MOLYBDATES; PROTEINS; RESOLUTION; SUBSTRATES; SULFATES; TRANSPORT; TUNGSTATES

Citation Formats

Tirado-Lee, Leidamarie, Lee, Allen, Rees, Douglas C., Pinkett, Heather W., and NWU). Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA. United States: N. p., 2014. Web. doi:10.1016/j.str.2011.10.004.
Tirado-Lee, Leidamarie, Lee, Allen, Rees, Douglas C., Pinkett, Heather W., & NWU). Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA. United States. doi:10.1016/j.str.2011.10.004.
Tirado-Lee, Leidamarie, Lee, Allen, Rees, Douglas C., Pinkett, Heather W., and NWU). Thu . "Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA". United States. doi:10.1016/j.str.2011.10.004.
@article{osti_1034211,
title = {Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA},
author = {Tirado-Lee, Leidamarie and Lee, Allen and Rees, Douglas C. and Pinkett, Heather W. and NWU)},
abstractNote = {molA (HI1472) from H. influenzae encodes a periplasmic binding protein (PBP) that delivers substrate to the ABC transporter MolB{sub 2}C{sub 2} (formerly HI1470/71). The structures of MolA with molybdate and tungstate in the binding pocket were solved to 1.6 and 1.7 {angstrom} 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 {approx}100 {mu}M 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.},
doi = {10.1016/j.str.2011.10.004},
journal = {Structure},
number = (11) ; 11, 2011,
volume = 19,
place = {United States},
year = {Thu Oct 02 00:00:00 EDT 2014},
month = {Thu Oct 02 00:00:00 EDT 2014}
}