Xanthomonins I-III: A New Class of Lasso Peptides with a Seven-Residue Macrolactam Ring

被引：69

作者：

Hegemann, Julian D. ^{[1
,2
]}

Zimmermann, Marcel ^{[1
,2
]}

Zhu, Shaozhou ^{[1
,2
]}

Steuber, Holger ^{[1
,2
]}

Harms, Klaus ^{[1
,2
]}

Xie, Xiulan ^{[1
,2
]}

Marahiel, Mohamed A. ^{[1
,2
]}

机构：

[1] Univ Marburg, Fachgebiet Biochem, Fachbereich Chem, D-35032 Marburg, Germany

[2] Univ Marburg, LOEWE Zentrum Synthet Mikrobiol, D-35032 Marburg, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2014年 / 53卷 / 08期

关键词：

biosynthesis; lasso peptides; macrocycles; natural products; steric hindrance; BACTERIAL RNA-POLYMERASE; STREPTOMYCES SP RE-701; MICROCIN J25; LEADER PEPTIDE; SIAMYCIN-II; ANTAGONIST; FERMENTATION; INHIBITOR; RES-701-1; SEQUENCE;

D O I：

10.1002/anie.201309267

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Lasso peptides belong to the class of ribosomally synthesized and post-translationally modified peptides. Their common distinguishing feature is an N-terminal macrolactam ring that is threaded by the C-terminal tail. This lasso fold is maintained through steric interactions. The isolation and characterization of xanthomoninsI-III, the first lasso peptides featuring macrolactam rings consisting of only seven amino acids, is now presented. The crystal structure of xanthomoninI and the NMR structure of xanthomoninII were also determined. A total of 25 variants of xanthomoninII were generated to probe different aspects of the biosynthesis, stability, and fold maintenance. These mutational studies reveal the limits such a small ring imposes on the threading and show that every plug amino acid larger than serine is able to maintain a heat-stable lasso fold in the xanthomoninII scaffold.

引用

页码：2230 / 2234

页数：5

共 41 条

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