1rwu
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1rwu.gif|left|200px]] | [[Image:1rwu.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1rwu", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1rwu| PDB=1rwu | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''Solution structure of conserved protein YbeD from E. coli''' | '''Solution structure of conserved protein YbeD from E. coli''' | ||
| Line 29: | Line 26: | ||
[[Category: Kozlov, G.]] | [[Category: Kozlov, G.]] | ||
[[Category: NESG, Northeast Structural Genomics Consortium.]] | [[Category: NESG, Northeast Structural Genomics Consortium.]] | ||
| - | [[Category: | + | [[Category: Mixed alpha-beta fold]] |
| - | [[Category: | + | [[Category: Nesg]] |
| - | [[Category: | + | [[Category: Northeast structural genomics consortium]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:00:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:00, 3 May 2008
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 Sat May 3 08:00:03 2008
