4C4V

Structure of the outer membrane protein insertase BamA with one POTRA domain.

4C4V の概要

• エントリーDOI: 10.2210/pdb4c4v/pdb
• 分子名称: OUTER MEMBRANE PROTEIN ASSEMBLY FACTOR BAMA (3 entities in total)
• 機能のキーワード: protein transport, omp85 superfamily
• 由来する生物種: ESCHERICHIA COLI; 詳細
• 細胞内の位置: Cell outer membrane: P0A940 P0A940
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104609.85

構造登録者

Zeth, K.,Albrecht, R.,Diederichs, K. (登録日: 2013-09-09, 公開日: 2014-04-23, 最終更新日: 2024-05-08)

主引用文献

Albrecht, R.,Schuetz, M.,Oberhettinger, P.,Faulstich, M.,Bermejo, I.,Rudel, T.,Diederichs, K.,Zeth, K.
Structure of Bama, an Essential Factor in Outer Membrane Protein Biogenesis
Acta Crystallogr.,Sect.D, 70:1779-, 2014

PubMed Abstract: Outer membrane protein (OMP) biogenesis is an essential process for maintaining the bacterial cell envelope and involves the β-barrel assembly machinery (BAM) for OMP recognition, folding and assembly. In Escherichia coli this function is orchestrated by five proteins: the integral outer membrane protein BamA of the Omp85 superfamily and four associated lipoproteins. To unravel the mechanism underlying OMP folding and insertion, the structure of the E. coli BamA β-barrel and P5 domain was determined at 3 Å resolution. These data add information beyond that provided in the recently published crystal structures of BamA from Haemophilus ducreyi and Neisseria gonorrhoeae and are a valuable basis for the interpretation of pertinent functional studies. In an `open' conformation, E. coli BamA displays a significant degree of flexibility between P5 and the barrel domain, which is indicative of a multi-state function in substrate transfer. E. coli BamA is characterized by a discontinuous β-barrel with impaired β1-β16 strand interactions denoted by only two connecting hydrogen bonds and a disordered C-terminus. The 16-stranded barrel surrounds a large cavity which implies a function in OMP substrate binding and partial folding. These findings strongly support a mechanism of OMP biogenesis in which substrates are partially folded inside the barrel cavity and are subsequently released laterally into the lipid bilayer.

PubMed: 24914988
DOI: 10.1107/S1399004714007482

実験手法

X-RAY DIFFRACTION (3 Å)