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PDBsum entry 4ld7
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PDB id:
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Transferase
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Title:
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Crystal structure of anapt from neosartorya fischeri
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Structure:
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Dimethylallyl tryptophan synthase. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p. Synonym: anapt. Engineered: yes
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Source:
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Neosartorya fischeri. Organism_taxid: 36630. Gene: nfia_055300. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.83Å
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R-factor:
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0.203
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R-free:
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0.202
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Authors:
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G.Zocher,T.Stehle
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Key ref:
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X.Yu
et al.
(2013).
Catalytic mechanism of stereospecific formation of cis-configured prenylated pyrroloindoline diketopiperazines by indole prenyltransferases.
Chem Biol,
20,
1492-1501.
PubMed id:
DOI:
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Date:
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24-Jun-13
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Release date:
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11-Dec-13
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PROCHECK
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Headers
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References
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A1DN10
(ANAPT_NEOFI) -
Indole diterpene prenyltransferase anaPT from Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181)
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Seq:
Struc:
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437 a.a.
397 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Chem Biol
20:1492-1501
(2013)
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PubMed id:
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Catalytic mechanism of stereospecific formation of cis-configured prenylated pyrroloindoline diketopiperazines by indole prenyltransferases.
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X.Yu,
G.Zocher,
X.Xie,
M.Liebhold,
S.Schütz,
T.Stehle,
S.M.Li.
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ABSTRACT
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Indole prenyltransferases AnaPT, CdpC3PT, and CdpNPT are known to catalyze the
formation of prenylated pyrroloindoline diketopiperazines from
tryptophan-containing cyclic dipeptides in one-step reactions. In this study, we
investigated the different stereoselectivities of these enzymes toward all the
stereoisomers of cyclo-Trp-Ala and cyclo-Trp-Pro. The stereoselectivities of
AnaPT and CdpC3PT mainly depend on the configuration of the tryptophanyl moiety
in the substrates, and they usually introduce the prenyl moiety from the
opposite sides. CdpNPT showed lower stereoselectivity, and the structure of the
second amino acid moiety in the substrates is important for the
stereospecificity in its enzyme catalysis. Moreover, we determined the crystal
structure of AnaPT in complex with thiolodiphosphate and compared it with the
known structures of CdpNPT. Our results clearly revealed the presence of an
indole binding mode that has so far not been characterized.
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