1iez
From Proteopedia
(New page: 200px<br /><applet load="1iez" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iez" /> '''Solution Structure of 3,4-Dihydroxy-2-Butano...) |
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| - | [[Image:1iez.gif|left|200px]]<br /><applet load="1iez" size=" | + | [[Image:1iez.gif|left|200px]]<br /><applet load="1iez" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iez" /> | caption="1iez" /> | ||
'''Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis'''<br /> | '''Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Recent developments in NMR have extended the size range of proteins | + | Recent developments in NMR have extended the size range of proteins amenable to structural and functional characterization to include many larger proteins involved in important cellular processes. By applying a combination of residue-specific isotope labeling and protein deuteration strategies tailored to yield specific information, we were able to determine the solution structure and study structure-activity relationships of 3,4-dihydroxy-2-butanone-4-phosphate synthase, a 47-kDa enzyme from the Escherichia coli riboflavin biosynthesis pathway and an attractive target for novel antibiotics. Our investigations of the enzyme's ligand binding by NMR and site-directed mutagenesis yields a conclusive picture of the location and identity of residues directly involved in substrate binding and catalysis. Our studies illustrate the power of state-of-the-art NMR techniques for the structural characterization and investigation of ligand binding in protein complexes approaching the 50-kDa range in solution. |
==About this Structure== | ==About this Structure== | ||
| - | 1IEZ 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:// | + | 1IEZ 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=1IEZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bacher, A.]] | [[Category: Bacher, A.]] | ||
| - | [[Category: Ball, L | + | [[Category: Ball, L J.]] |
| - | [[Category: Kelly, M | + | [[Category: Kelly, M J.S.]] |
[[Category: Kuhne, R.]] | [[Category: Kuhne, R.]] | ||
[[Category: Oschkinat, H.]] | [[Category: Oschkinat, H.]] | ||
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[[Category: structure based design]] | [[Category: structure based design]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:12 2008'' |
Revision as of 11:11, 21 February 2008
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Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis
Overview
Recent developments in NMR have extended the size range of proteins amenable to structural and functional characterization to include many larger proteins involved in important cellular processes. By applying a combination of residue-specific isotope labeling and protein deuteration strategies tailored to yield specific information, we were able to determine the solution structure and study structure-activity relationships of 3,4-dihydroxy-2-butanone-4-phosphate synthase, a 47-kDa enzyme from the Escherichia coli riboflavin biosynthesis pathway and an attractive target for novel antibiotics. Our investigations of the enzyme's ligand binding by NMR and site-directed mutagenesis yields a conclusive picture of the location and identity of residues directly involved in substrate binding and catalysis. Our studies illustrate the power of state-of-the-art NMR techniques for the structural characterization and investigation of ligand binding in protein complexes approaching the 50-kDa range in solution.
About this Structure
1IEZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site., Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S, Schmieder P, Kuhne R, Bermel W, Bacher A, Richter G, Oschkinat H, Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13025-30. Epub 2001 Oct 30. PMID:11687623
Page seeded by OCA on Thu Feb 21 13:11:12 2008
