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Article

Insights into dimerization and four-helix bundle formation found by dissection of the dimer interface of the GrpE protein from Escherichia coli.

Protein science : a publication of the Protein Society - 1 Jun 2003

Mehl Andrew F, Heskett Luke D, Jain Sumesh S, Demeler Borries

Abstract excerpt

The GrpE heat shock protein from Escherichia coli has a homodimeric structure. The dimer interface encompasses two long alpha-helices at the NH(2)-terminal end from each monomer (forming a "tail"), which lead into a small four-helix bundle from which each monomer contributes two short sequential alpha-helices in an antiparallel topological arrangement. We have created a number of different deletion mutants of...

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Identifiers

PMID: 12761391
DOI: 10.1110/ps.0300803
PMCID: PMC2323885

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