1rwu
From Proteopedia
(New page: 200px<br /><applet load="1rwu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rwu" /> '''Solution structure of conserved protein YbeD...) |
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| - | [[Image:1rwu.gif|left|200px]]<br /><applet load="1rwu" size=" | + | [[Image:1rwu.gif|left|200px]]<br /><applet load="1rwu" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of conserved protein YbeD from E. coli'''<br /> | '''Solution structure of conserved protein YbeD from E. coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Lipoic acid is an essential prosthetic group in several metabolic | + | 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== | ==About this Structure== | ||
| - | 1RWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1RWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C H.]] |
[[Category: Gehring, K.]] | [[Category: Gehring, K.]] | ||
[[Category: Kozlov, G.]] | [[Category: Kozlov, G.]] | ||
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: mixed alpha-beta fold]] | [[Category: mixed alpha-beta fold]] | ||
[[Category: nesg]] | [[Category: nesg]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:25 2008'' |
Revision as of 12:55, 21 February 2008
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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
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