Escherichia coli, protein structure-function

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Rychlewski, L., Zhang, B., and Godzik, A. (1999). Functional insights from structural predictions analysis of the Escherichia coli genome. Protein Sci. 8, 614-624. 

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The bacterium Escherichia coli produces more than 3,000 different proteins a human produces 25,000 to 35,000. In both cases, each type of protein has a unique three-dimensional structure and this structure confers a unique function. Each type of protein also has a unique amino acid sequence. Intuition suggests that the amino acid sequence must play a fundamental role in determining the three-dimensional structure of the protein, and ultimately its function, but is this supposition cor-... 

In an Escherichia coli expression system for the aqualysin I precursor, the precursor is processed autoproteolytically into the mature 28-kDa enzyme by treatment at 65 ° C.23) In this case, the N-terminal pro-sequence is required for the production of active enzyme and functions to stabilize the precursor structure.283 The C-terminal pro-sequence is not essential for the production of active aqualysin 1,293 but seems to be involved in the translocation of the precursor across the cytoplasmic membrane.303 In a Thermus thermophilus expression system,313 the C-terminal pro-sequence is required for the production and extracellular secretion of active aqualysin I.323 In an E. coli expression system for the subtilisin E gene, the N-terminal pro-sequence is essential for the production of active enzyme,333 as in the case of aqualysin I. The requirement of the pro-sequence is also shown in vitro for the refolding of the inactive mature protein to an active enzyme.34 353 The functions of the N-terminal pro-sequences of aqualysin I and subtilisin E seem to be similar. 

Koebnik, R. (1999). Structural and functional roles of the surface-exposed loops of the /3-barrel membrane protein OmpA from Escherichia coli.J. Baderiol. 181, 3688-3694. 

Nordlund, P., and Eklund, H., 1993, Structure and function of the Escherichia coli ribonucleotide reductase protein R2 J. Mol. Biol. 232 1239164. 

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