2PST

1.8A Crystal Structure of the PA2412 protein from Pseudomonas aeruginosa

2PST の概要

• エントリーDOI: 10.2210/pdb2pst/pdb
• 関連するPDBエントリー: 2GPF
• 分子名称: Hypothetical protein PA2412 (2 entities in total)
• 機能のキーワード: pyoverdine synthesis, non-ribosomal peptide synthesis clusters, mbth-like family, cog3251, unknown function
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8649.74

構造登録者

Gulick, A.M.,Drake, E.J.,Shah, M.B. (登録日: 2007-05-07, 公開日: 2007-05-22, 最終更新日: 2024-02-21)

主引用文献

Drake, E.J.,Cao, J.,Qu, J.,Shah, M.B.,Straubinger, R.M.,Gulick, A.M.
The 1.8 A crystal structure of PA2412, an MbtH-like protein from the pyoverdine cluster of Pseudomonas aeruginosa.
J.Biol.Chem., 282:20425-20434, 2007

PubMed Abstract: Many bacteria use nonribosomal peptide synthetase (NRPS) proteins to produce peptide antibiotics and siderophores. The catalytic domains of the NRPS proteins are usually linked in large multidomain proteins. Often, additional proteins are coexpressed with NRPS proteins that modify the NRPS peptide products, ensure the availability of substrate building blocks, or play a role in the import or export of the NRPS product. Many NRPS clusters include a small protein of approximately 80 amino acids with homology to the MbtH protein of mycobactin synthesis in Mycobacteria tuberculosis; no function has been assigned to these proteins. Pseudomonas aeruginosa utilizes an NRPS cluster to synthesize the siderophore pyoverdine. The pyoverdine peptide contains a dihydroxyquinoline-based chromophore, as well as two formyl-N-hydroxyornithine residues, which are involved in iron binding. The pyoverdine cluster contains four modular NRPS enzymes and 10-15 additional proteins that are essential for pyoverdine production. Coexpressed with the pyoverdine synthetic enzymes is a 72-amino acid MbtH-like family member designated PA2412. We have determined the three-dimensional structure of the PA2412 protein and describe here the structure and the location of conserved regions. Additionally, we have further analyzed a deletion mutant of the PA2412 protein for growth and pyoverdine production. Our results demonstrate that PA2412 is necessary for the production or secretion of pyoverdine at normal levels. The PA2412 deletion strain is able to use exogenously produced pyoverdine, showing that there is no defect in the uptake or utilization of the iron-pyoverdine complex.

PubMed: 17502378
DOI: 10.1074/jbc.M611833200

実験手法

X-RAY DIFFRACTION (1.8 Å)