title: Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas.
abstract: Cupins form one of the most functionally diverse superfamilies of proteins, with members performing a wide range of catalytic, non-catalytic, and regulatory functions. HutD is a predicted bicupin protein that is involved in histidine utilization (Hut) in Pseudomonas species. Previous genetic analyses have suggested that it limits the upper level of Hut pathway expression, but its mechanism of action is unknown. Here, we have determined the structure of PfluHutD at 1.74 Å resolution in several crystallization conditions, and identified N-formyl-l-glutamate (FG, a Hut pathway intermediate) as a potential ligand in vivo. Proteins 2017; 85:1580-1588. © 2017 Wiley Periodicals, Inc.
authors.affiliation: New Zealand Institute for Advanced Study, Massey University Albany, Auckland, New Zealand.
authors.forename: M L
authors.initials: ML
authors.lastname: Gerth
authors.affiliation: New Zealand Institute for Advanced Study, Massey University Albany, Auckland, New Zealand.
authors.forename: Y
authors.initials: Y
authors.lastname: Liu
authors.affiliation: Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.
authors.forename: W
authors.initials: W
authors.lastname: Jiao
authors.affiliation: New Zealand Institute for Advanced Study, Massey University Albany, Auckland, New Zealand.
authors.forename: X-X
authors.initials: XX
authors.lastname: Zhang
authors.affiliation: School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand, New Zealand.
authors.forename: E N
authors.initials: EN
authors.lastname: Baker
authors.affiliation: School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand, New Zealand.
authors.forename: J S
authors.initials: JS
authors.lastname: Lott
authors.affiliation: New Zealand Institute for Advanced Study, Massey University Albany, Auckland, New Zealand.|Ecole Supérieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI ParisTech), CNRS UMR 8231, PSL Research University, Paris Cedex 05, 75231, France.|Department of Microbial Population Biology, Max Planck Institute for Evolutionary Biology, August-Thiennemann Strasse 2, Plön, 24306, Germany.
authors.forename: P B
authors.initials: PB
authors.lastname: Rainey
authors.affiliation: School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand, New Zealand.
authors.forename: J M
authors.identifier: http://orcid.org/0000-0003-4895-0243
authors.initials: JM
authors.lastname: Johnston
mesh_terms: D020816:Amino Acid Motifs; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D001692:Biological Transport; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D005971:Glutamates / Q000737:chemistry* / Q000378:metabolism; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D011551:Pseudomonas fluorescens / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D005971:Glutamates; D011994:Recombinant Proteins; C053697:N-formylglutamate; D006639:Histidine
keywords: crystal structure; cupin; ligand binding