X-ray Crystal Structure of Teicoplanin A2-2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy

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We report the X-ray crystal structure of a site-selective peptide catalyst moiety and teicoplanin A2-2 complex. The expressed protein ligation technique was used to couple T4 lysozyme (T4L) and a synthetic peptide catalyst responsible for the selective phosphorylation of the N-acetylglucosamine sugar in a teicoplanin A2-2 derivative. The T4L-Pmh-dPro-Aib-dAla-dAla construct was crystallized in the presence of teicoplanin A2-2. The resulting 2.3 Å resolution protein–peptide–teicoplanin complex crystal structure revealed that the nucleophilic nitrogen of N-methylimidazole in the Pmh residue is in closer proximity (7.6 Å) to the N-acetylglucosamine than the two other sugar rings present in teicoplanin (9.3 and 20.3 Å, respectively). This molecular arrangement is consistent with the observed selectivity afforded by the peptide-based catalyst when it is applied to a site-selective phosphorylation reaction involving a teicoplanin A2-2 derivative.
Publisher
AMER CHEMICAL SOC
Issue Date
2014-08
Language
English
Article Type
Article
Keywords

ASYMMETRIC PHOSPHORYLATION; CARDIAC GLYCOSIDE; HAIRPIN FORMATION; ANTIBIOTICS; VANCOMYCIN; LIGATION; COMPLEX; DEOXYGENATION; SEMISYNTHESIS; GLYCOPEPTIDE

Citation

JOURNAL OF ORGANIC CHEMISTRY, v.79, no.18, pp.8550 - 8556

ISSN
0022-3263
DOI
10.1021/jo501625f
URI
http://hdl.handle.net/10203/201084
Appears in Collection
CH-Journal Papers(저널논문)
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