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HisE11 and HisF8 provide bis-histidyl heme hexa-coordination in the globin domain of Geobacter sulfurreducens globin-coupled sensor.

Pesce A, Thijs L, Nardini M, Desmet F, Sisinni L, Gourlay L, Bolli A, Coletta M, Van Doorslaer S, Wan X, Alam M, Ascenzi P, Moens L, Bolognesi M, Dewilde S
J Mol Biol 386 246-60 (2009)
Cited: 28 times
EuropePMC logo PMID: 19109973

Abstract

Among heme-based sensors, recent phylogenomic and sequence analyses have identified 34 globin coupled sensors (GCS), to which an aerotactic or gene-regulating function has been tentatively ascribed. Here, the structural and biochemical characterization of the globin domain of the GCS from Geobacter sulfurreducens (GsGCS(162)) is reported. A combination of X-ray crystallography (crystal structure at 1.5 A resolution), UV-vis and resonance Raman spectroscopy reveals the ferric GsGCS(162) as an example of bis-histidyl hexa-coordinated GCS. In contrast to the known hexa-coordinated globins, the distal heme-coordination in ferric GsGCS(162) is provided by a His residue unexpectedly located at the E11 topological site. Furthermore, UV-vis and resonance Raman spectroscopy indicated that ferrous deoxygenated GsGCS(162) is a penta-/hexa-coordinated mixture, and the heme hexa-to-penta-coordination transition does not represent a rate-limiting step for carbonylation kinetics. Lastly, electron paramagnetic resonance indicates that ferrous nitrosylated GsGCS(162) is a penta-coordinated species, where the proximal HisF8-Fe bond is severed.

Reviews - 2w31 mentioned but not cited (2)

  1. Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxis. Martínková M, Kitanishi K, Shimizu T. J. Biol. Chem. 288 27702-27711 (2013)
  2. Conservation of the three-dimensional structure in non-homologous or unrelated proteins. Sousounis K, Haney CE, Cao J, Sunchu B, Tsonis PA. Hum. Genomics 6 10 (2012)

Articles - 2w31 mentioned but not cited (6)

  1. Structure and properties of a bis-histidyl ligated globin from Caenorhabditis elegans. Yoon J, Herzik MA, Winter MB, Tran R, Olea C, Marletta MA. Biochemistry 49 5662-5670 (2010)
  2. Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber. Ilcu L, Röther W, Birke J, Brausemann A, Einsle O, Jendrossek D. Sci Rep 7 6179 (2017)
  3. Coordination and redox state-dependent structural changes of the heme-based oxygen sensor AfGcHK associated with intraprotein signal transduction. Stranava M, Man P, Skálová T, Kolenko P, Blaha J, Fojtikova V, Martínek V, Dohnálek J, Lengalova A, Rosůlek M, Shimizu T, Martínková M. J. Biol. Chem. 292 20921-20935 (2017)
  4. Disruption of the dimerization interface of the sensing domain in the dimeric heme-based oxygen sensor AfGcHK abolishes bacterial signal transduction. Skalova T, Lengalova A, Dohnalek J, Harlos K, Mihalcin P, Kolenko P, Stranava M, Blaha J, Shimizu T, Martínková M. J Biol Chem 295 1587-1597 (2020)
  5. Structural modeling of a novel membrane-bound globin-coupled sensor in Geobacter sulfurreducens. Hammerschmid D, Germani F, Drusin SI, Fagnen C, Schuster CD, Hoogewijs D, Marti MA, Venien-Bryan C, Moens L, Van Doorslaer S, Sobott F, Dewilde S. Comput Struct Biotechnol J 19 1874-1888 (2021)
  6. The Vibrio vulnificus stressosome is an oxygen-sensor involved in regulating iron metabolism. Heinz V, Jäckel W, Kaltwasser S, Cutugno L, Bedrunka P, Graf A, Reder A, Michalik S, Dhople VM, Madej MG, Conway M, Lechner M, Riedel K, Bange G, Boyd A, Völker U, Lewis RJ, Marles-Wright J, Ziegler C, Pané-Farré J. Commun Biol 5 622 (2022)


Reviews citing this publication (3)

  1. Structural heterogeneity and ligand gating in ferric Methanosarcina acetivorans protoglobin mutants. Pesce A, Tilleman L, Dewilde S, Ascenzi P, Coletta M, Ciaccio C, Bruno S, Moens L, Bolognesi M, Nardini M. IUBMB Life 63 287-294 (2011)
  2. Mechanism and Role of Globin-Coupled Sensor Signalling. Walker JA, Rivera S, Weinert EE. Adv. Microb. Physiol. 71 133-169 (2017)
  3. Rubber oxygenases. Jendrossek D, Birke J. Appl. Microbiol. Biotechnol. 103 125-142 (2019)

Articles citing this publication (17)

  1. Bacterial and archaeal globins - a revised perspective. Vinogradov SN, Tinajero-Trejo M, Poole RK, Hoogewijs D. Biochim. Biophys. Acta 1834 1789-1800 (2013)
  2. Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5. Kitanishi K, Kobayashi K, Uchida T, Ishimori K, Igarashi J, Shimizu T. J. Biol. Chem. 286 35522-35534 (2011)
  3. Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase. Hannibal L, Collins D, Brassard J, Chakravarti R, Vempati R, Dorlet P, Santolini J, Dawson JH, Stuehr DJ. Biochemistry 51 8514-8529 (2012)
  4. A redox signalling globin is essential for reproduction in Caenorhabditis elegans. De Henau S, Tilleman L, Vangheel M, Luyckx E, Trashin S, Pauwels M, Germani F, Vlaeminck C, Vanfleteren JR, Bert W, Pesce A, Nardini M, Bolognesi M, De Wael K, Moens L, Dewilde S, Braeckman BP. Nat Commun 6 8782 (2015)
  5. Structural analysis of an oxygen-regulated diguanylate cyclase. Tarnawski M, Barends TR, Schlichting I. Acta Crystallogr. D Biol. Crystallogr. 71 2158-2177 (2015)
  6. A phylogenetic analysis of the globins in fungi. Hoogewijs D, Dewilde S, Vierstraete A, Moens L, Vinogradov SN. PLoS ONE 7 e31856 (2012)
  7. Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination. Nothnagel HJ, Preimesberger MR, Pond MP, Winer BY, Adney EM, Lecomte JT. J. Biol. Inorg. Chem. 16 539-552 (2011)
  8. Ligand- and proton-linked conformational changes of the ferrous 2/2 hemoglobin of Pseudoalteromonas haloplanktis TAC125. Giordano D, Russo R, Ciaccio C, Howes BD, di Prisco G, Marden MC, Hui Bon Hoa G, Smulevich G, Coletta M, Verde C. IUBMB Life 63 566-573 (2011)
  9. (1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state. Pond MP, Vuletich DA, Falzone CJ, Majumdar A, Lecomte JT. Biomol NMR Assign 3 211-214 (2009)
  10. Structural characterization of the heme-based oxygen sensor, AfGcHK, its interactions with the cognate response regulator, and their combined mechanism of action in a bacterial two-component signaling system. Stranava M, Martínek V, Man P, Fojtikova V, Kavan D, Vaněk O, Shimizu T, Martinkova M. Proteins 84 1375-1389 (2016)
  11. Structure and haem-distal site plasticity in Methanosarcina acetivorans protoglobin. Pesce A, Tilleman L, Donné J, Aste E, Ascenzi P, Ciaccio C, Coletta M, Moens L, Viappiani C, Dewilde S, Bolognesi M, Nardini M. PLoS ONE 8 e66144 (2013)
  12. Introduction of water into the heme distal side by Leu65 mutations of an oxygen sensor, YddV, generates verdoheme and carbon monoxide, exerting the heme oxygenase reaction. Stranava M, Martínková M, Stiborová M, Man P, Kitanishi K, Muchová L, Vítek L, Martínek V, Shimizu T. J. Inorg. Biochem. 140 29-38 (2014)
  13. Open and Lys-His Hexacoordinated Closed Structures of a Globin with Swapped Proximal and Distal Sites. Teh AH, Saito JA, Najimudin N, Alam M. Sci Rep 5 11407 (2015)
  14. Research Support, Non-U.S. Gov't Crystal structure of Kumaglobin: a hexacoordinated heme protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus. Kim J, Fukuda Y, Inoue T. FEBS J 286 1287-1304 (2019)
  15. Functional and structural roles of the N-terminal extension in Methanosarcina acetivorans protoglobin. Ciaccio C, Pesce A, Tundo GR, Tilleman L, Bertolacci L, Dewilde S, Moens L, Ascenzi P, Bolognesi M, Nardini M, Coletta M. Biochim. Biophys. Acta 1834 1813-1823 (2013)
  16. Probing the ligand recognition and discrimination environment of the globin-coupled oxygen sensor protein YddV by FTIR and time-resolved step-scan FTIR spectroscopy. Pavlou A, Martínková M, Shimizu T, Kitanishi K, Stranava M, Loullis A, Pinakoulaki E. Phys Chem Chem Phys 17 17007-17015 (2015)
  17. A bioinformatics insight to rhizobial globins: gene identification and mapping, polypeptide sequence and phenetic analysis, and protein modeling. Gesto-Borroto R, Sánchez-Sánchez M, Arredondo-Peter R. F1000Res 4 117 (2015)


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