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PDBsum entry 2vee
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Transport protein
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PDB id
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2vee
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure of protoglobin from methanosarcina acetivorans c2a
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Structure:
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Protoglobin. Chain: a, b, c, d, e, f, g, h. Engineered: yes. Mutation: yes
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Source:
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Methanosarcina acetivorans. Organism_taxid: 2214. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.60Å
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R-factor:
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0.208
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R-free:
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0.263
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Authors:
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M.Nardini,A.Pesce,L.Thijs,J.A.Saito,S.Dewilde,M.Alam,P.Ascenzi, M.Coletta,C.Ciaccio,L.Moens,M.Bolognesi
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Key ref:
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M.Nardini
et al.
(2008).
Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity.
Embo Rep,
9,
157-163.
PubMed id:
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Date:
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22-Oct-07
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Release date:
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22-Jan-08
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PROCHECK
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Headers
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References
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Q8TLY9
(Q8TLY9_METAC) -
Globin-sensor domain-containing protein from Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
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Seq:
Struc:
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195 a.a.
190 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Embo Rep
9:157-163
(2008)
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PubMed id:
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Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity.
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M.Nardini,
A.Pesce,
L.Thijs,
J.A.Saito,
S.Dewilde,
M.Alam,
P.Ascenzi,
M.Coletta,
C.Ciaccio,
L.Moens,
M.Bolognesi.
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ABSTRACT
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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 1.3 A 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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Storbeck,
S.Rolfes,
E.Raux-Deery,
M.J.Warren,
D.Jahn,
and
G.Layer
(2010).
A novel pathway for the biosynthesis of heme in Archaea: genome-based bioinformatic predictions and experimental evidence.
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Archaea,
2010,
175050.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
