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PDBsum entry 6t6x
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References listed in PDB file
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Key reference
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Title
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The bottromycin epimerase both defines a group of atypical α/β-Hydrolase-Fold enzymes.
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Authors
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A.Sikandar,
L.Franz,
S.Adam,
J.Santos-Aberturas,
L.Horbal,
A.Luzhetskyy,
A.W.Truman,
O.V.Kalinina,
J.Koehnke.
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Ref.
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Nat Chem Biol, 2020,
16,
1013-1018.
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PubMed id
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Abstract
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D-amino acids endow peptides with diverse, desirable properties, but the
post-translational and site-specific epimerization of L-amino acids into their
D-counterparts is rare and chemically challenging. Bottromycins are ribosomally
synthesized and post-translationally modified peptides that have overcome this
challenge and feature a D-aspartate (D-Asp), which was proposed to arise
spontaneously during biosynthesis. We have identified the highly unusual
α/β-hydrolase (ABH) fold enzyme BotH as a peptide epimerase responsible for
the post-translational epimerization of L-Asp to D-Asp during bottromycin
biosynthesis. The biochemical characterization of BotH combined with the
structures of BotH and the BotH-substrate complex allowed us to propose a
mechanism for this reaction. Bioinformatic analyses of BotH homologs show that
similar ABH enzymes are found in diverse biosynthetic gene clusters. This places
BotH as the founding member of a group of atypical ABH enzymes that may be able
to epimerize non-Asp stereocenters across different families of secondary
metabolites.
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Secondary reference #1
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Title
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Towards automated crystallographic structure refinement with phenix.Refine.
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Authors
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P.V.Afonine,
R.W.Grosse-Kunstleve,
N.Echols,
J.J.Headd,
N.W.Moriarty,
M.Mustyakimov,
T.C.Terwilliger,
A.Urzhumtsev,
P.H.Zwart,
P.D.Adams.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2012,
68,
352-367.
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PubMed id
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