ArticleJournal of bacteriology2002
The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Contributions of Conformational Flexibility to High-Affinity Zinc Binding in the Solute Binding Protein AztC.ACS omega · 2022Article
- Comparison of transcriptional profiles of Treponema pallidum during experimental infection of rabbits and in vitro culture: Highly similar, yet different.PLoS pathogens · 2021Article
- Article
- How Zinc-Binding Systems, Expressed by Human Pathogens, Acquire Zinc from the Colonized Host Environment: A Critical Review on Zincophores.Current medicinal chemistry · 2021Review
- Structural Features Mediating Zinc Binding and Transfer in the AztABCD Zinc Transporter System.Biomolecules · 2020Article
- Article
- Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity.Journal of bacteriology · 2020Article
- Structures of the substrate-binding protein YfeA in apo and zinc-reconstituted holo forms.Acta crystallographica. Section D, Structural biology · 2019Article
- Essential Metal Uptake in Gram-negative Bacteria: X-ray Fluorescence, Radioisotopes, and Cell Fractionation.Journal of visualized experiments : JoVE · 2018Article
- The crystal structure of the Yersinia pestis iron chaperone YiuA reveals a basic triad binding motif for the chelated metal.Acta crystallographica. Section D, Structural biology · 2017Article
- Mechanisms of zinc binding to the solute-binding protein AztC and transfer from the metallochaperone AztD.The Journal of biological chemistry · 2017Article
- Transcriptional and Physiological Changes during Mycobacterium tuberculosis Reactivation from Non-replicating Persistence.Frontiers in microbiology · 2016Article
- Manganese uptake and streptococcal virulence.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
- Host-imposed manganese starvation of invading pathogens: two routes to the same destination.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
- Transcriptional Regulation, Metal Binding Properties and Structure of Pden1597, an Unusual Zinc Transport Protein from Paracoccus denitrificans.The Journal of biological chemistry · 2015Article
- Apo, Zn2+-bound and Mn2+-bound structures reveal ligand-binding properties of SitA from the pathogen Staphylococcus pseudintermedius.Bioscience reports · 2014Article
- Imperfect coordination chemistry facilitates metal ion release in the Psa permease.Nature chemical biology · 2014Article
- MntABC and MntH contribute to systemic Staphylococcus aureus infection by competing with calprotectin for nutrient manganese.Infection and immunity · 2013Article
- Allosteric inhibition of a zinc-sensing transcriptional repressor: insights into the arsenic repressor (ArsR) family.Journal of molecular biology · 2013Article
- Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story.Life (Basel, Switzerland) · 2013Review
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Abstract
We previously demonstrated that Treponema pallidum TroA is a periplasmic metal-binding protein (MBP) with a distinctive alpha-helical backbone. To better understand the mechanisms of metal binding and release by TroA, we determined the crystal structure of the apoprotein at a resolution of 2.5 A and compared it to that of the Zn(II)-bound form (Protein Data Bank accession code 1toa). apo-TroA shows a conformation even more closed than that of its Zn(II)-bound counterpart due to a 4 degrees tilt of the C-terminal domain (residues 190 through 308) about an axis parallel to the poorly flexible backbone helix. This domain tilting pushes two loops (residues 248 through 253 and 277 through 286) towards the metal-binding site by more than 1 A, resulting in an unfavorable interaction of I251 with D66. To avoid this contact, D66 shifts towards H68, one of the four Zn(II)-coordinating residues. The approach of this negative charge coincides with the flipping of the imidazole side chain of H68, resulting in the formation of a new hydrogen bond. The conformational change of H68, along with a slight rearrangement of D279, a C-terminal domain Zn(II)-coordinating residue, distorts the metal-binding site geometry, presumably causing the release of the bound metal ion. Ligand binding and release by TroA, and presumably by other members of the MBP cluster, differs from the "Venus flytrap" mechanism utilized by bacterial nonmetal solute-binding receptors.
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