Structural highlights
1rwu is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Gene: | YBED, B0631, C0721, Z0776, ECS0669, SF0650, S0672 ("Bacillus coli" Migula 1895) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lipoic acid is an essential prosthetic group in several metabolic pathways. The biosynthetic pathway of protein lipoylation in Escherichia coli involves gene products of the lip operon. YbeD is a conserved bacterial protein located in the dacA-lipB intergenic region. Here, we report the nuclear magnetic resonance structure of YbeD from E. coli. The structure includes a beta alpha beta beta alpha beta fold with two alpha-helices on one side of a four-strand antiparallel beta-sheet. The beta 2-beta 3 loop shows the highest sequence conservation and is likely functionally important. The beta-sheet surface contains a patch of conserved hydrophobic residues, suggesting a role in protein-protein interactions. YbeD shows striking structural homology to the regulatory domain from d-3-phosphoglycerate dehydrogenase, hinting at a role in the allosteric regulation of lipoic acid biosynthesis or the glycine cleavage system.
Structural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains.,Kozlov G, Elias D, Semesi A, Yee A, Cygler M, Gehring K J Bacteriol. 2004 Dec;186(23):8083-8. PMID:15547281[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kozlov G, Elias D, Semesi A, Yee A, Cygler M, Gehring K. Structural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains. J Bacteriol. 2004 Dec;186(23):8083-8. PMID:15547281 doi:http://dx.doi.org/186/23/8083
