5L22

PrtD T1SS ABC transporter

5L22 の概要

• エントリーDOI: 10.2210/pdb5l22/pdb
• 分子名称: ABC transporter (HlyB subfamily), ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: t1ss, abc transporter, atpase, secretion, protein transport
• 由来する生物種: Aquifex aeolicus (strain VF5)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 129385.15

構造登録者

Morgan, J.L.W.,Zimmer, J. (登録日: 2016-07-30, 公開日: 2017-03-08, 最終更新日: 2024-03-06)

主引用文献

Morgan, J.L.,Acheson, J.F.,Zimmer, J.
Structure of a Type-1 Secretion System ABC Transporter.
Structure, 25:522-529, 2017

PubMed Abstract: Type-1 secretion systems (T1SSs) represent a widespread mode of protein secretion across the cell envelope in Gram-negative bacteria. The T1SS is composed of an inner-membrane ABC transporter, a periplasmic membrane-fusion protein, and an outer-membrane porin. These three components assemble into a complex spanning both membranes and providing a conduit for the translocation of unfolded polypeptides. We show that ATP hydrolysis and assembly of the entire T1SS complex is necessary for protein secretion. Furthermore, we present a 3.15-Å crystal structure of AaPrtD, the ABC transporter found in the Aquifex aeolicus T1SS. The structure suggests a substrate entry window just above the transporter's nucleotide binding domains. In addition, highly kinked transmembrane helices, which frame a narrow channel not observed in canonical peptide transporters, are likely involved in substrate translocation. Overall, the AaPrtD structure supports a polypeptide transport mechanism distinct from alternating access.

PubMed: 28216041
DOI: 10.1016/j.str.2017.01.010

実験手法

X-RAY DIFFRACTION (3.15 Å)