Structural basis for the heme transfer reaction in heme uptake machinery from Corynebacteria

2019 ◽  
Vol 55 (92) ◽  
pp. 13864-13867
Author(s):  
Norifumi Muraki ◽  
Chihiro Kitatsuji ◽  
Yasunori Okamoto ◽  
Takeshi Uchida ◽  
Koichiro Ishimori ◽  
...  
Keyword(s):  
Transfer Reaction ◽  
Structural Basis ◽  
Heme Binding ◽  
Heme Uptake ◽  
Heme Transfer

The CR domains in HtaA and HtaB are responsible for heme binding/transport in the heme-uptake machinery in Corynebacteria.

scholarly journals Structural basis for heme-dependent NCoR binding to the transcriptional repressor REV-ERBβ

2021 ◽  
Vol 7 (5) ◽  
pp. eabc6479
Author(s):  
Sarah A. Mosure ◽  
Timothy S. Strutzenberg ◽  
Jinsai Shang ◽  
Paola Munoz-Tello ◽  
Laura A. Solt ◽  
...  
Keyword(s):  
Nuclear Receptors ◽  
Binding Mode ◽  
Structural Basis ◽  
Receptor Interaction ◽  
Heme Binding ◽  
Endogenous Ligand ◽  
Interaction Domain ◽  
Response Elements ◽  
Biochemical Assays ◽  
Chemical Cross Linking

Heme is the endogenous ligand for the constitutively repressive REV-ERB nuclear receptors, REV-ERBα (NR1D1) and REV-ERBβ (NR1D2), but how heme regulates REV-ERB activity remains unclear. Cellular studies indicate that heme is required for the REV-ERBs to bind the corepressor NCoR and repress transcription. However, fluorescence-based biochemical assays suggest that heme displaces NCoR; here, we show that this is due to a heme-dependent artifact. Using ITC and NMR spectroscopy, we show that heme binding remodels the thermodynamic interaction profile of NCoR receptor interaction domain (RID) binding to REV-ERBβ ligand-binding domain (LBD). We solved two crystal structures of REV-ERBβ LBD cobound to heme and NCoR peptides, revealing the heme-dependent NCoR binding mode. ITC and chemical cross-linking mass spectrometry reveals a 2:1 LBD:RID stoichiometry, consistent with cellular studies showing that NCoR-dependent repression of REV-ERB transcription occurs on dimeric DNA response elements. Our findings should facilitate renewed progress toward understanding heme-dependent REV-ERB activity.

Structural Basis of Hydrogenotrophic Methanogenesis

2020 ◽  
Vol 74 (1) ◽  
pp. 713-733
Author(s):  
Seigo Shima ◽  
Gangfeng Huang ◽  
Tristan Wagner ◽  
Ulrich Ermler
Keyword(s):  
Transfer Reaction ◽  
Catalytic Mechanism ◽  
Methanogenic Archaea ◽  
Energy Coupling ◽  
Structural Basis ◽  
Biomass Degradation ◽  
Hydrogenotrophic Methanogenesis ◽  
Sufficient Energy ◽  
Ion Gradient ◽  
Electron Reduction

Most methanogenic archaea use the rudimentary hydrogenotrophic pathway—from CO2 and H2 to methane—as the terminal step of microbial biomass degradation in anoxic habitats. The barely exergonic process that just conserves sufficient energy for a modest lifestyle involves chemically challenging reactions catalyzed by complex enzyme machineries with unique metal-containing cofactors. The basic strategy of the methanogenic energy metabolism is to covalently bind C1 species to the C1 carriers methanofuran, tetrahydromethanopterin, and coenzyme M at different oxidation states. The four reduction reactions from CO2 to methane involve one molybdopterin-based two-electron reduction, two coenzyme F420–based hydride transfers, and one coenzyme F430–based radical process. For energy conservation, one ion-gradient-forming methyl transfer reaction is sufficient, albeit supported by a sophisticated energy-coupling process termed flavin-based electron bifurcation for driving the endergonic CO2 reduction and fixation. Here, we review the knowledge about the structure-based catalytic mechanism of each enzyme of hydrogenotrophic methanogenesis.

scholarly journals Heme Transfer from Streptococcal Cell Surface Protein Shp to HtsA of Transporter HtsABC

2005 ◽  
Vol 73 (8) ◽  
pp. 5086-5092 ◽  
Author(s):  
Mengyao Liu ◽  
Benfang Lei
Keyword(s):  
Cell Surface ◽  
Abc Transporter ◽  
Group A Streptococcus ◽  
Polyacrylamide Gel Electrophoresis ◽  
Surface Protein ◽  
Heme Binding ◽  
Cell Surface Protein ◽  
Heme Acquisition ◽  
Native Polyacrylamide Gel Electrophoresis ◽  
Heme Transfer

ABSTRACT Human pathogen group A streptococcus (GAS) can take up heme from host heme-containing proteins as a source of iron. Little is known about the heme acquisition mechanism in GAS. We recently identified a streptococcal cell surface protein (designated Shp) and the lipoprotein component (designated HtsA) of an ATP-binding cassette (ABC) transporter made by GAS as heme-binding proteins. In an effort to delineate the molecular mechanism involved in heme acquisition by GAS, heme-free Shp (apo-Shp) and HtsA (apo-HtsA) were used to investigate heme transfer from heme-containing proteins (holo proteins) to the apo proteins. In addition, the interaction between holo-Shp and holo-HtsA was examined using native polyacrylamide gel electrophoresis. Heme was efficiently transferred from holo-Shp to apo-HtsA but not from holo-HtsA to apo-Shp. Apo-Shp acquired heme from human hemoglobin, and holo-Shp and holo-HtsA were able to form a complex, suggesting that Shp actively relays heme from hemoglobin to apo-HtsA. These findings demonstrate for the first time complex formation and directional heme transfer between a cell surface heme-binding protein and the lipoprotein of a heme-specific ABC transporter in gram-positive bacteria.

Thermodynamics of Heme Binding to the HasASMHemophore:  Effect of Mutations at Three Key Residues for Heme Uptake†

Biochemistry ◽  
2003 ◽  
Vol 42 (36) ◽  
pp. 10627-10633 ◽  
Author(s):  
Clarisse Deniau ◽  
Robert Gilli ◽  
Nadia Izadi-Pruneyre ◽  
Sylvie Létoffé ◽  
Muriel Delepierre ◽  
...  
Keyword(s):  
Heme Binding ◽  
Heme Uptake ◽  
Key Residues

Characterization of the Periplasmic Heme-Binding Protein ShuT from the Heme Uptake System ofShigella dysenteriae†

Biochemistry ◽  
2005 ◽  
Vol 44 (39) ◽  
pp. 13179-13191 ◽  
Author(s):  
Suntara Eakanunkul ◽  
Gudrun S. Lukat-Rodgers ◽  
Suganya Sumithran ◽  
Arundhati Ghosh ◽  
Kenton R. Rodgers ◽  
...  
Keyword(s):  
Binding Protein ◽  
Uptake System ◽  
Heme Binding ◽  
Heme Uptake ◽  
Heme Binding Protein

scholarly journals A Pivotal Heme-transfer Reaction Intermediate in CytochromecBiogenesis

2011 ◽  
Vol 287 (4) ◽  
pp. 2342-2352 ◽  
Author(s):  
Despoina A. I. Mavridou ◽  
Julie M. Stevens ◽  
Leonie Mönkemeyer ◽  
Oliver Daltrop ◽  
Katalin di Gleria ◽  
...  
Keyword(s):  
Transfer Reaction ◽  
Reaction Intermediate ◽  
Heme Transfer
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