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PDBsum entry 5wkp
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396 a.a.
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81 a.a.
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72 a.a.
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118 a.a.
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126 a.a.
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PDB id:
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Transferase
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Title:
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Crystal structure of the human mitochondrial cysteine desulfurase in complex with isd11 and iron-sulfur cluster scaffold protein iscu1, and e. Coli acp1 protein at 3.15a
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Structure:
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Cysteine desulfurase, mitochondrial. Chain: a, e. Fragment: unp residues 56-457. Engineered: yes. Lyr motif-containing protein 4. Chain: b, f. Engineered: yes. Acyl carrier protein. Chain: c, g.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: nfs1, nifs, hussy-08. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: lyrm4, c6orf149, isd11, cgi-203. Escherichia coli. Organism_taxid: 562.
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Resolution:
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3.15Å
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R-factor:
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0.190
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R-free:
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0.243
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Authors:
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M.T.Boniecki,M.Cygler
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Key ref:
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M.T.Boniecki
et al.
(2017).
Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.
Nat Commun,
8,
1287.
PubMed id:
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Date:
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25-Jul-17
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Release date:
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15-Nov-17
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PROCHECK
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Headers
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References
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Q9Y697
(NFS1_HUMAN) -
Cysteine desulfurase from Homo sapiens
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Seq:
Struc:
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457 a.a.
396 a.a.*
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Q9HD34
(LYRM4_HUMAN) -
LYR motif-containing protein 4 from Homo sapiens
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Seq:
Struc:
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91 a.a.
81 a.a.*
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P0A6A8
(ACP_ECOLI) -
Acyl carrier protein from Escherichia coli (strain K12)
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Seq:
Struc:
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78 a.a.
72 a.a.
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Enzyme class 2:
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Chains A, E:
E.C.2.8.1.7
- cysteine desulfurase.
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Reaction:
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(sulfur carrier)-H + L-cysteine = (sulfur carrier)-SH + L-alanine
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(sulfur carrier)-H
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+
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L-cysteine
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=
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(sulfur carrier)-SH
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+
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L-alanine
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Cofactor:
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Pyridoxal 5'-phosphate
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Pyridoxal 5'-phosphate
Bound ligand (Het Group name =
PLP)
matches with 93.75% similarity
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Enzyme class 3:
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Chains B, C, D, F, G, H:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Nat Commun
8:1287
(2017)
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PubMed id:
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Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.
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M.T.Boniecki,
S.A.Freibert,
U.Mühlenhoff,
R.Lill,
M.Cygler.
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ABSTRACT
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Iron-sulfur (Fe/S) clusters are essential protein cofactors crucial for many
cellular functions including DNA maintenance, protein translation, and energy
conversion. De novo Fe/S cluster synthesis occurs on the mitochondrial scaffold
protein ISCU and requires cysteine desulfurase NFS1, ferredoxin, frataxin, and
the small factors ISD11 and ACP (acyl carrier protein). Both the mechanism of
Fe/S cluster synthesis and function of ISD11-ACP are poorly understood. Here, we
present crystal structures of three different NFS1-ISD11-ACP complexes with and
without ISCU, and we use SAXS analyses to define the 3D architecture of the
complete mitochondrial Fe/S cluster biosynthetic complex. Our structural and
biochemical studies provide mechanistic insights into Fe/S cluster synthesis at
the catalytic center defined by the active-site Cys of NFS1 and conserved Cys,
Asp, and His residues of ISCU. We assign specific regulatory rather than
catalytic roles to ISD11-ACP that link Fe/S cluster synthesis with mitochondrial
lipid synthesis and cellular energy status.
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