UniProt release 5.8
Published August 30, 2005
Escherichia coli inner membrane proteome
We have integrated into UniProtKB/Swiss-Prot the results obtained by Gunnar von Heijne's group on the inner membrane proteome of Escherichia coli (see Daley D.O. et al. , Science 308:1321-3, 2005; PubMed ID: 15919996).
von Heijne's group has applied the PhoA/GFP fusion approach to derive topology models for almost the entire E. coli inner membrane proteome. More than 500 entries concerning membrane proteins had their subcellular location updated and the topology added.
Integral membrane proteins account for the coding capacity of 20 to 30% of the genes in typical organisms and are critically important for many cellular functions. However, owing to their hydrophobic and amphiphilic nature, membrane proteins are difficult to study, and they account for less than 1% of the known high-resolution protein structures. Overexpression, purification, biochemical analysis, and structure determination are all far more challenging than for soluble proteins, and membrane proteins have rarely been considered in proteomics or structural genomics contexts to date.
Changes concerning keywords