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PDBsum entry 4xvx
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Oxidoreductase
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PDB id
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4xvx
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Crystal structure of an acyl-acp dehydrogenase
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Structure:
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Acyl-[acyl-carrier-protein] dehydrogenase mbtn. Chain: a, b. Synonym: acyl-acp dehydrogenase mbtn,mycobactin synthase protein n. Engineered: yes
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Source:
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Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: mbtn, fade14, rv1346, mtcy02b10.10. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.30Å
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R-factor:
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0.176
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R-free:
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0.212
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Authors:
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A.Chai,J.M.Johnston,R.D.Bunker,J.S.Lott,E.N.Baker,Tb Structural Genomics Consortium (Tbsgc)
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Key ref:
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A.F.Chai
et al.
(2015).
A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket.
Acta Crystallogr D Biol Crystallogr,
71,
862-872.
PubMed id:
DOI:
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Date:
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28-Jan-15
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Release date:
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11-Feb-15
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Supersedes:
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PROCHECK
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Headers
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References
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P9WQF9
(MBTN_MYCTU) -
Acyl-[acyl-carrier-protein] dehydrogenase MbtN from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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Seq:
Struc:
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386 a.a.
371 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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DOI no:
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Acta Crystallogr D Biol Crystallogr
71:862-872
(2015)
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PubMed id:
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A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket.
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A.F.Chai,
E.M.Bulloch,
G.L.Evans,
J.S.Lott,
E.N.Baker,
J.M.Johnston.
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ABSTRACT
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Mycobacterium tuberculosis (Mtb) is the causative agent of tuberculosis. Access
to iron in host macrophages depends on iron-chelating siderophores called
mycobactins and is strongly correlated with Mtb virulence. Here, the crystal
structure of an Mtb enzyme involved in mycobactin biosynthesis, MbtN, in complex
with its FAD cofactor is presented at 2.30 Å resolution. The polypeptide fold
of MbtN conforms to that of the acyl-CoA dehydrogenase (ACAD) family, consistent
with its predicted role of introducing a double bond into the acyl chain of
mycobactin. Structural comparisons and the presence of an acyl carrier protein,
MbtL, in the same gene locus suggest that MbtN acts on an acyl-(acyl carrier
protein) rather than an acyl-CoA. A notable feature of the crystal structure is
the tubular density projecting from N(5) of FAD. This was interpreted as a
covalently bound polyethylene glycol (PEG) fragment and resides in a hydrophobic
pocket where the substrate acyl group is likely to bind. The pocket could
accommodate an acyl chain of 14-21 C atoms, consistent with the expected length
of the mycobactin acyl chain. Supporting this, steady-state kinetics show that
MbtN has ACAD activity, preferring acyl chains of at least 16 C atoms. The
acyl-binding pocket adopts a different orientation (relative to the FAD) to
other structurally characterized ACADs. This difference may be correlated with
the apparent ability of MbtN to catalyse the formation of an unusual cis double
bond in the mycobactin acyl chain.
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Links
