Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity

Autor: Marco Nardini, Liesbet Thijs, Martino Bolognesi, Paolo Ascenzi, Alessandra Pesce, Maqsudul Alam, Sylvia Dewilde, Jennifer A. Saito, L. Moens, M. Coletta, Chiara Ciaccio
Přispěvatelé: Nardini, M, Pesce, A, Thijs, L, Saito, Ja, Dewilde, S, Alam, M, Ascenzi, Paolo, Coletta, M, Ciaccio, C, Moens, L, Bolognesi, M.
Jazyk: angličtina
Rok vydání: 2008
Předmět:
Models
Molecular
molecular cloning
Secondary
HEMOGLOBINS
matrix protein
Crystallography
X-Ray
Ligands
Biochemistry
bacterial protein
Protein Structure
Secondary
Diffusion
Models
Carbon Monoxide
Crystallography
Cytoglobin
globin
article
hemoprotein
BINDING PROPERTIES
protein function
Ligand (biochemistry)
Transport protein
priority journal
Neuroglobin
Methanosarcina
Thermodynamics
mutagenesis
crystal structure
Protein Structure
Stereochemistry
Methanosarcina acetivorans
ligand binding
Archaeal Proteins
Scientific Report
protein localization
Heme
Biology
BACILLUS-SUBTILIS
OXYGEN-BINDING
nitric oxide
Genetics
Globin
Settore BIO/10
Molecular Biology
protein expression
nonhuman
carbon dioxide
cytoglobin
Molecular
nucleotide sequence
hemoglobin
biology.organism_classification
protein family
Archaea
Globin fold
neuroglobin
oxygen
protoglobin
amino terminal sequence
protein determination
protein structure
Kinetics
Oxygen
Helix
X-Ray
Human medicine
Zdroj: EMBO reports
9 (2008): 157–163.
info:cnr-pdr/source/autori:Nardini, M; Pesce, A; Thijs, L; Saito, JA; Dewilde, S; Alam, M; Ascenzi, P; Coletta, M; Ciaccio, C; Moens, L; Bolognesi, M/titolo:Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity/doi:/rivista:EMBO reports (Print)/anno:2008/pagina_da:157/pagina_a:163/intervallo_pagine:157–163/volume:9
ISSN: 1469-221X
Popis: The structural adaptability of the globin fold has been highlighted by the recent discovery of the 2-on-2 haemoglobins, of neuroglobin and cytoglobin. Protoglobin from Methanosarcina acetivorans C2A - a strictly anaerobic methanogenic Archaea - is, to the best of our knowledge, the latest entry adding new variability and functional complexity to the haemoglobin (Hb) superfamily. Here, we report the 11.3 angstrom crystal structure of oxygenated M. acetivorans protoglobin, together with the first insight into its ligand-binding properties. We show that, contrary to all known globins, protoglobin-specific loops and an amino-terminal extension completely bury the haem within the protein matrix. Access of O-2, CO and NO to the haem is granted by the protoglobin-specific apolar tunnels reaching the haem distal site from locations at the B/G and B/E helix interfaces. Functionally, M. acetivorans dimeric protoglobin shows a selectivity ratio for O-2/CO binding to the haem that favours O-2 ligation and anticooperativity in ligand binding. Both properties are exceptional within the Hb superfamily.
Databáze: OpenAIRE
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