1RWU

Solution structure of conserved protein YbeD from E. coli

Summary for 1RWU

• Entry DOI: 10.2210/pdb1rwu/pdb
• NMR Information: BMRB: 6102
• Descriptor: Hypothetical UPF0250 protein ybeD (1 entity in total)
• Functional Keywords: mixed alpha-beta fold, structural genomics, protein structure initiative, psi, northeast structural genomics consortium, nesg, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 12422.07

Authors

Kozlov, G.,Arrowsmith, C.H.,Gehring, K.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2003-12-17, release date: 2004-12-21, Last modification date: 2024-05-22)

Primary citation

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., 186:8083-8088, 2004

PubMed Abstract: 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.

PubMed: 15547281
DOI: 10.1128/JB.186.23.8083-8088.2004

Experimental method

SOLUTION NMR