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PDBsum entry 1v9q
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Oxygen storage/transport
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PDB id
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1v9q
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Contents |
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* Residue conservation analysis
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PDB id:
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Oxygen storage/transport
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Title:
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Crystal structure of an artificial metalloprotein:mn(iii)(3,3'-me2- salophen)/apo-a71g myoglobin
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Structure:
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Myoglobin. Chain: a. Engineered: yes. Mutation: yes
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Source:
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Physeter catodon. Sperm whale. Organism_taxid: 9755. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.45Å
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R-factor:
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0.206
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R-free:
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0.218
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Authors:
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T.Ueno,T.Koshiyama,M.Kono,K.Kondo,M.Ohashi,A.Suzuki,T.Yamane, Y.Watanabe
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Key ref:
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T.Ueno
et al.
(2005).
Coordinated design of cofactor and active site structures in development of new protein catalysts.
J Am Chem Soc,
127,
6556-6562.
PubMed id:
DOI:
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Date:
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29-Jan-04
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Release date:
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17-May-05
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PROCHECK
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Headers
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References
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P02185
(MYG_PHYMC) -
Myoglobin from Physeter macrocephalus
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Seq:
Struc:
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154 a.a.
154 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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DOI no:
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J Am Chem Soc
127:6556-6562
(2005)
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PubMed id:
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Coordinated design of cofactor and active site structures in development of new protein catalysts.
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T.Ueno,
T.Koshiyama,
M.Ohashi,
K.Kondo,
M.Kono,
A.Suzuki,
T.Yamane,
Y.Watanabe.
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ABSTRACT
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New methods for the synthesis of artificial metalloenzymes are important for the
construction of novel biocatalysts and biomaterials. Recently, we reported new
methodology for the synthesis of artificial metalloenzymes by reconstituting
apo-myoglobin with metal complexes (Ohashi, M. et al., Angew Chem., Int. Ed.
2003, 42, 1005-1008). However, it has been difficult to improve their
reactivity, since their crystal structures were not available. In this article,
we report the crystal structures of M(III)(Schiff base).apo-A71GMbs (M = Cr and
Mn). The structures suggest that the position of the metal complex in apo-Mb is
regulated by (i) noncovalent interaction between the ligand and surrounding
peptides and (ii) the ligation of the metal ion to proximal histidine (His93).
In addition, it is proposed that specific interactions of Ile107 with 3- and
3'-substituent groups on the salen ligand control the location of the Schiff
base ligand in the active site. On the basis of these results, we have
successfully controlled the enantioselectivity in the sulfoxidation of
thioanisole by changing the size of substituents at the 3 and 3' positions. This
is the first example of an enantioselective enzymatic reaction regulated by the
design of metal complex in the protein active site.
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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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F.Jiang,
and
W.Ding
(2011).
PVMR: assembling small helix fragments as structural solutions for molecular replacement.
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Acta Crystallogr A,
67,
56-62.
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O.Shoji,
and
Y.Watanabe
(2011).
Design of H2O2-dependent oxidation catalyzed by hemoproteins.
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Metallomics,
3,
379-388.
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A.Dalla Cort,
P.De Bernardin,
G.Forte,
and
F.Y.Mihan
(2010).
Metal-salophen-based receptors for anions.
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Chem Soc Rev,
39,
3863-3874.
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V.Köhler,
and
T.R.Ward
(2010).
Design of a functional nitric oxide reductase within a myoglobin scaffold.
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Chembiochem,
11,
1049-1051.
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C.A.Kruithof,
A.Berger,
H.P.Dijkstra,
F.Soulimani,
T.Visser,
M.Lutz,
A.L.Spek,
R.J.Gebbink,
and
G.van Koten
(2009).
Sulfato-bridged ECE-pincer palladium(II) complexes: structures in the solid-state and in solution, and catalytic properties.
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Dalton Trans,
(),
3306-3314.
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C.H.Kuo,
L.Fruk,
and
C.M.Niemeyer
(2009).
Addressable DNA-myoglobin photocatalysis.
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Chem Asian J,
4,
1064-1069.
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C.L.Davies,
E.L.Dux,
and
A.K.Duhme-Klair
(2009).
Supramolecular interactions between functional metal complexes and proteins.
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Dalton Trans,
(),
10141-10154.
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J.L.Zhang,
D.K.Garner,
L.Liang,
D.A.Barrios,
and
Y.Lu
(2009).
Noncovalent modulation of pH-dependent reactivity of a Mn-salen cofactor in myoglobin with hydrogen peroxide.
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Chemistry,
15,
7481-7489.
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P.Rousselot-Pailley,
C.Bochot,
C.Marchi-Delapierre,
A.Jorge-Robin,
L.Martin,
J.C.Fontecilla-Camps,
C.Cavazza,
and
S.Ménage
(2009).
The protein environment drives selectivity for sulfide oxidation by an artificial metalloenzyme.
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Chembiochem,
10,
545-552.
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A.Pordea,
and
T.R.Ward
(2008).
Chemogenetic protein engineering: an efficient tool for the optimization of artificial metalloenzymes.
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Chem Commun (Camb),
(),
4239-4249.
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H.Takashima,
E.Fujimoto,
C.Hirai,
and
K.Tsukahara
(2008).
Synthesis and spectroscopic properties of reconstituted zinc-myoglobin appending a DNA-binding platinum(II) complex.
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Chem Biodivers,
5,
2101-2112.
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J.L.Zhang,
D.K.Garner,
L.Liang,
Q.Chen,
and
Y.Lu
(2008).
Protein scaffold of a designed metalloenzyme enhances the chemoselectivity in sulfoxidation of thioanisole.
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Chem Commun (Camb),
(),
1665-1667.
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J.Niemeyer,
S.Abe,
T.Hikage,
T.Ueno,
G.Erker,
and
Y.Watanabe
(2008).
Noncovalent insertion of ferrocenes into the protein shell of apo-ferritin.
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Chem Commun (Camb),
(),
6519-6521.
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N.Yokoi,
T.Ueno,
M.Unno,
T.Matsui,
M.Ikeda-Saito,
and
Y.Watanabe
(2008).
Ligand design for the improvement of stability of metal complex.protein hybrids.
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Chem Commun (Camb),
(),
229-231.
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PDB code:
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T.Koshiyama,
N.Yokoi,
T.Ueno,
S.Kanamaru,
S.Nagano,
Y.Shiro,
F.Arisaka,
and
Y.Watanabe
(2008).
Molecular design of heteroprotein assemblies providing a bionanocup as a chemical reactor.
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Small,
4,
50-54.
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PDB code:
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G.Roelfes
(2007).
DNA and RNA induced enantioselectivity in chemical synthesis.
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Mol Biosyst,
3,
126-135.
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M.Creus,
and
T.R.Ward
(2007).
Designed evolution of artificial metalloenzymes: protein catalysts made to order.
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Org Biomol Chem,
5,
1835-1844.
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C.Letondor,
and
T.R.Ward
(2006).
Artificial metalloenzymes for enantioselective catalysis: recent advances.
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Chembiochem,
7,
1845-1852.
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M.T.Reetz,
and
N.Jiao
(2006).
Copper-phthalocyanine conjugates of serum albumins as enantioselective catalysts in Diels-Alder reactions.
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Angew Chem Int Ed Engl,
45,
2416-2419.
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T.Ueno,
N.Yokoi,
M.Unno,
T.Matsui,
Y.Tokita,
M.Yamada,
M.Ikeda-Saito,
H.Nakajima,
and
Y.Watanabe
(2006).
Design of metal cofactors activated by a protein-protein electron transfer system.
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Proc Natl Acad Sci U S A,
103,
9416-9421.
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PDB codes:
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Y.Lu
(2006).
Biosynthetic inorganic chemistry.
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Angew Chem Int Ed Engl,
45,
5588-5601.
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Y.Lu
(2006).
Metalloprotein and metallo-DNA/RNAzyme design: current approaches, success measures, and future challenges.
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Inorg Chem,
45,
9930-9940.
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C.A.Kruithof,
M.A.Casado,
G.Guillena,
M.R.Egmond,
A.van der Kerk-van Hoof,
A.J.Heck,
R.J.Klein Gebbink,
and
G.van Koten
(2005).
Lipase active-site-directed anchoring of organometallics: metallopincer/protein hybrids.
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Chemistry,
11,
6869-6877.
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G.Klein,
N.Humbert,
J.Gradinaru,
A.Ivanova,
F.Gilardoni,
U.E.Rusbandi,
and
T.R.Ward
(2005).
Tailoring the active site of chemzymes by using a chemogenetic-optimization procedure: towards substrate-specific artificial hydrogenases based on the biotin-avidin technology.
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Angew Chem Int Ed Engl,
44,
7764-7767.
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M.Skander,
C.Malan,
A.Ivanova,
and
T.R.Ward
(2005).
Chemical optimization of artificial metalloenzymes based on the biotin-avidin technology: (S)-selective and solvent-tolerant hydrogenation catalysts via the introduction of chiral amino acid spacers.
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Chem Commun (Camb),
(),
4815-4817.
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
