Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of <i>Legionella pneumophila</i>

Petermann, N.; Hansen, Guido; Schmidt, Christian; Hilgenfeld, Rolf

doi:10.1016/j.febslet.2009.12.045

Cited by 29 publications

(27 citation statements)

References 31 publications

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“…Further, significant limitations to studying Feo structure by crystallography have been observed, since a consensus on the oligomeric state of FeoB has never been reached. For example, FeoB N-terminal domains from several organisms have crystallized as monomers (35,53,(55)(56)(57) whereas the FeoB N-terminal domains from other organisms have crystallized as dimers or trimers (51)(52)(53)(54). Since those studies used a truncated FeoB protein, interactions involving the membrane-spanning regions or C terminus of FeoB were not detected.…”

Section: Discussionmentioning

confidence: 99%

“…The switch II region of GTPases undergoes a conformational change upon GTP binding, and in Legionella pneumophila, mutations in this region of FeoB cause a decrease in FeoB nucleotide binding (35,50). The V. cholerae FeoB D72A mutation was unable to promote growth of EPV6 without heme, indicating that the D72A mutation resulted in loss of function.…”

Section: Fig 4 V Cholerae Feob Makes Higher-order Native Complexes Amentioning

confidence: 96%

“…Alignment of V. cholerae FeoB with p21-Ras suggests that the G4 motif, which provides guanine base specificity (35), is positioned at amino acids 119 to 122 (Fig. 1B).…”

Section: Fig 4 V Cholerae Feob Makes Higher-order Native Complexes Amentioning

confidence: 99%

“…1B and C). The G5 motif is the least conserved motif and has been identified in FeoB through structural analysis but not through sequence alignments (33,35). These G motifs are necessary for binding and hydrolysis of the guanine nucleotide (36)(37)(38).…”

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Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex

2016

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Feo is the major ferrous iron transport system in prokaryotes. Despite having been discovered over 25 years ago and found to be widely distributed among bacteria, Feo is poorly understood, as its structure and mechanism of iron transport have not been determined. The feo operon in Vibrio cholerae is made up of three genes, encoding the FeoA, FeoB, and FeoC proteins, which are all required for Feo system function. FeoA and FeoC are both small cytoplasmic proteins, and their function remains unclear. FeoB, which is thought to function as a ferrous iron permease, is a large integral membrane protein made up of an N-terminal GTPase domain and a C-terminal membrane-spanning region. To date, structural studies of FeoB have been carried out using a truncated form of the protein encompassing only the N-terminal GTPase region. In this report, we show that full-length FeoB forms higher-order complexes when cross-linked in vivo in V. cholerae. Our analysis of these complexes revealed that FeoB can simultaneously associate with both FeoA and FeoC to form a large complex, an observation that has not been reported previously. We demonstrate that interactions between FeoB and FeoA, but not between FeoB and FeoC, are required for complex formation. Additionally, we identify amino acid residues in the GTPase region of FeoB that are required for function of the Feo system and for complex formation. These observations suggest that this large Feo complex may be the active form of Feo that is used for ferrous iron transport. IMPORTANCEThe Feo system is the major route for ferrous iron transport in bacteria. In this work, the Vibrio cholerae Feo proteins, FeoA, FeoB, and FeoC, are shown to interact to form a large inner membrane complex in vivo. This is the first report showing an interaction among all three Feo proteins. It is also determined that FeoA, but not FeoC, is required for Feo complex assembly. Iron is an indispensable component of enzymes involved in a wide range of biological processes and, as a result, is essential for life in almost all organisms (1). Notwithstanding the fact that iron is abundant in nature, aerobic, neutral-pH environments favor the formation of Fe(OH) 3 , a highly insoluble ferric iron (Fe 3ϩ ) complex. In contrast, in anoxic environments, free ferrous iron (Fe 2ϩ ) is more readily available (2). In order to meet their iron requirement, bacteria have multiple iron transport systems that allow use of the various forms of iron present in their environment, and Vibrio cholerae is no exception (3).V. cholerae is a human pathogen that causes cholera, a severe diarrheal disease resulting from the ingestion of contaminated food or water (4). V. cholerae must acquire iron from different environments, such as the gut of its human host or the fresh, brackish, and ocean waters that make up its natural habitat. This need to acquire the various forms of iron is reflected in the observation that approximately 1% of its genome is devoted to the acquisition of iron (3). In V. cholerae, ferric iron is commo...

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Section: Discussionmentioning

confidence: 99%

Section: Fig 4 V Cholerae Feob Makes Higher-order Native Complexes Amentioning

confidence: 96%

“…Alignment of V. cholerae FeoB with p21-Ras suggests that the G4 motif, which provides guanine base specificity (35), is positioned at amino acids 119 to 122 (Fig. 1B).…”

Section: Fig 4 V Cholerae Feob Makes Higher-order Native Complexes Amentioning

confidence: 99%

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confidence: 99%

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Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex

2016

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“…To gain further insight into the mechanism of FeoB, we and other groups have recently structurally characterized the soluble G protein domain from four different organisms: E. coli, Methanococcus jannaschii, Thermotoga maritima, and Legionella pneumophilia (9,(13)(14)(15). The structures revealed a canonical G protein similar to Ras, followed by a helical domain with a proposed effector (9) or GDP dissociation inhibitor role (8,13).…”

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confidence: 99%