5NJ9

E. coli Microcin-processing metalloprotease TldD/E with DRVY angiotensin fragment bound

5NJ9 の概要

• エントリーDOI: 10.2210/pdb5nj9/pdb
• 分子名称: Metalloprotease TldD, Metalloprotease PmbA, ASP-ARG-VAL-TYR, ... (8 entities in total)
• 機能のキーワード: metalloprotease, microcin, ccda, dna gyrase, hydrolase
• 由来する生物種: Escherichia coli K-12; 詳細
• 細胞内の位置: Cytoplasm: P0AFK0
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 205755.63

構造登録者

Ghilarov, D.,Serebryakova, M.,Stevenson, C.E.M.,Hearnshaw, S.J.,Volkov, D.,Maxwell, A.,Lawson, D.M.,Severinov, K. (登録日: 2017-03-28, 公開日: 2017-10-04, 最終更新日: 2024-01-17)

主引用文献

Ghilarov, D.,Serebryakova, M.,Stevenson, C.E.M.,Hearnshaw, S.J.,Volkov, D.S.,Maxwell, A.,Lawson, D.M.,Severinov, K.
The Origins of Specificity in the Microcin-Processing Protease TldD/E.
Structure, 25:1549-1561.e5, 2017

PubMed Abstract: TldD and TldE proteins are involved in the biosynthesis of microcin B17 (MccB17), an Escherichia coli thiazole/oxazole-modified peptide toxin targeting DNA gyrase. Using a combination of biochemical and crystallographic methods we show that E. coli TldD and TldE interact to form a heterodimeric metalloprotease. TldD/E cleaves the N-terminal leader sequence from the modified MccB17 precursor peptide, to yield mature antibiotic, while it has no effect on the unmodified peptide. Both proteins are essential for the activity; however, only the TldD subunit forms a novel metal-containing active site within the hollow core of the heterodimer. Peptide substrates are bound in a sequence-independent manner through β sheet interactions with TldD and are likely cleaved via a thermolysin-type mechanism. We suggest that TldD/E acts as a "molecular pencil sharpener": unfolded polypeptides are fed through a narrow channel into the active site and processively truncated through the cleavage of short peptides from the N-terminal end.

PubMed: 28943336
DOI: 10.1016/j.str.2017.08.006

実験手法

X-RAY DIFFRACTION (1.25 Å)