|SMART accession number:||SM00867|
|Description:||E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to polyisoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.|
|Interpro abstract (IPR007372):|
This entry represents the lipid-binding protein YceI from Escherichia coli [(PUBMED:12107143)] and the polyisoprenoid-binding protein TTHA0802 from Thermus thermophilus [(PUBMED:15741337)]. Both these proteins share a common domain with an 8-stranded beta-barrel fold, which resembles the lipocalin fold, although no sequence homology exists with lipocalins. In TTHA0802, the protein binds the polyisoprenoid chain within the pore of the barrel via hydrophobic interactions [(PUBMED:15741337)]. Sequence homologues of this core structure are present in a wide range of bacteria and archaea. The crystal structures of Yce1 and TTHA0802 suggest that this family of proteins plays an important role in isoprenoid quinone metabolism and/or transport and/or storage [(PUBMED:15741337)].
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