1rwu
From Proteopedia
| Line 8: | Line 8: | ||
|GENE= YBED, B0631, C0721, Z0776, ECS0669, SF0650, S0672 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= YBED, B0631, C0721, Z0776, ECS0669, SF0650, S0672 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK04998 PRK04998]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK04998 PRK04998]</span> | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwu OCA], [http://www.ebi.ac.uk/pdbsum/1rwu PDBsum | + | |RELATEDENTRY= |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwu OCA], [http://www.ebi.ac.uk/pdbsum/1rwu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rwu RCSB]</span> | ||
}} | }} | ||
| Line 35: | Line 36: | ||
[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:05 2008'' |
Revision as of 20:34, 30 March 2008
| |||||||
| Gene: | YBED, B0631, C0721, Z0776, ECS0669, SF0650, S0672 (Escherichia coli) | ||||||
| Domains: | PRK04998 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of conserved protein YbeD from E. coli
Overview
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.
About this Structure
1RWU is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 23:34:05 2008
