1.2 Å resolution crystal structure of the periplasmic aminotransferase PvdN from Pseudomonas aeruginosa

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• 作者：Eric J. Drake and Andrew M. Gulick
• 关键词：PvdN ; pyoverdine ; nonribosomal peptide synthetase ; Pseudomonas aeruginosa
• 刊名：Acta Crystallographica Section F
• 出版年：2016
• 出版时间：May 2016
• 年：2016
• 卷：72
• 期：5
• 页码：403-408
• 全文大小：1057K
• ISSN：1744-3091

文摘

The Gram-negative pathogen Pseudomonas aeruginosa uses a nonribosomal peptide synthetase (NRPS) biosynthetic cluster for the production of a peptide siderophore. In addition to four multimodular NRPS proteins, the biosynthetic pathway also requires several additional enzymes involved in the production of nonproteinogenic amino acids and maturation of the peptide product. Among the proteins that are required for the final steps in pyoverdine synthesis is PvdN, a pyridoxal phosphate-dependent enzyme that catalyzes an uncharacterized step in pyoverdine production. This study reports the high-resolution structure of PvdN bound to a PLP cofactor solved by multi-wavelength anomalous dispersion (MAD). The PvdN model shows high structural homology to type I aspartate aminotransferases and also contains positive density that suggests an uncharacterized external aldimine.