6NSI

Crystal structure of Fe(III)-bound YtgA from Chlamydia trachomatis

Summary for 6NSI

• Entry DOI: 10.2210/pdb6nsi/pdb
• Descriptor: Manganese-binding protein, FE (III) ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: ytga, solute-binding protein, chlamydia trachomatis, iron acquisition, abc transporter, metal binding protein
• Biological source: Chlamydia trachomatis
• Total number of polymer chains: 1
• Total formula weight: 32836.89

Authors

Luo, Z.,Campbell, R.,Begg, S.L.,Kobe, B.,McDevitt, C.A. (deposition date: 2019-01-24, release date: 2019-10-30, Last modification date: 2023-10-11)

Primary citation

Luo, Z.,Neville, S.L.,Campbell, R.,Morey, J.R.,Menon, S.,Thomas, M.,Eijkelkamp, B.A.,Ween, M.P.,Huston, W.M.,Kobe, B.,McDevitt, C.A.
Structure and Metal Binding Properties of Chlamydia trachomatis YtgA.
J.Bacteriol., 202:-, 2019

PubMed Abstract: The obligate intracellular pathogen is a globally significant cause of sexually transmitted bacterial infections and the leading etiological agent of preventable blindness. The first-row transition metal iron (Fe) plays critical roles in chlamydial cell biology, and acquisition of this nutrient is essential for the survival and virulence of the pathogen. Nevertheless, how acquires Fe from host cells is not well understood, since it lacks genes encoding known siderophore biosynthetic pathways, receptors for host Fe storage proteins, and the Fe acquisition machinery common to many bacteria. Recent studies have suggested that directly acquires host Fe via the ATP-binding cassette permease YtgABCD. Here, we characterized YtgA, the periplasmic solute binding protein component of the transport pathway, which has been implicated in scavenging Fe(III) ions. The structure of Fe(III)-bound YtgA was determined at 2.0-Å resolution with the bound ion coordinated via a novel geometry (3 Ns, 2 Os [3N2O]). This unusual coordination suggested a highly plastic metal binding site in YtgA capable of interacting with other cations. Biochemical analyses showed that the metal binding site of YtgA was not restricted to interaction with only Fe(III) ions but could bind all transition metal ions examined. However, only Mn(II), Fe(II), and Ni(II) ions bound reversibly to YtgA, with Fe being the most abundant cellular transition metal in Collectively, these findings show that YtgA is the metal-recruiting component of the YtgABCD permease and is most likely involved in the acquisition of Fe(II) and Mn(II) from host cells. is the most common bacterial sexually transmitted infection in developed countries, with an estimated global prevalence of 4.2% in the 15- to 49-year age group. Although infection is asymptomatic in more than 80% of infected women, about 10% of cases result in serious disease. Infection by is dependent on the ability to acquire essential nutrients, such as the transition metal iron, from host cells. In this study, we show that iron is the most abundant transition metal in and report the structural and biochemical properties of the iron-recruiting protein YtgA. Knowledge of the high-resolution structure of YtgA will provide a platform for future structure-based antimicrobial design approaches.

PubMed: 31611288
DOI: 10.1128/JB.00580-19

Experimental method

X-RAY DIFFRACTION (2.00006345565 Å)