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High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli.

ABSTRACT: In Escherichia coli, the BAM complex is employed to mediate correct folding of the outer membrane (OM) proteins into ?-barrels and their insertion into the OM. BamA, which is an essential component of the complex, consists of a C-terminal transmembrane region and five N-terminal polypeptide transport-associated (POTRA) domains. Although deletion studies have shown that each of the POTRA domains plays an important role in the process of BAM complex formation, only POTRA5 is essential for cell viability. Here, the crystal structure of POTRA4-5 has been determined to 1.50?Å resolution with an R factor of 14.7% and an Rfree of 18.9%.

SUBMITTER: Zhang H

PROVIDER: S-EPMC3144785 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli.

Zhang Heng H Gao Zeng-Qiang ZQ Hou Hai-Feng HF Xu Jian-Hua JH Li Lan-Fen LF Su Xiao-Dong XD Dong Yu-Hui YH

Acta crystallographica. Section F, Structural biology and crystallization communications 20110623 Pt 7

In Escherichia coli, the BAM complex is employed to mediate correct folding of the outer membrane (OM) proteins into β-barrels and their insertion into the OM. BamA, which is an essential component of the complex, consists of a C-terminal transmembrane region and five N-terminal polypeptide transport-associated (POTRA) domains. Although deletion studies have shown that each of the POTRA domains plays an important role in the process of BAM complex formation, only POTRA5 is essential for cell via ...[more]

PMID: 21795783

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