1y8b
From Proteopedia
(New page: 200px<br /><applet load="1y8b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y8b" /> '''Solution NMR-Derived Global Fold of Malate S...) |
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'''Solution NMR-Derived Global Fold of Malate Synthase G from E.coli'''<br /> | '''Solution NMR-Derived Global Fold of Malate Synthase G from E.coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The size of proteins that can be studied by solution NMR spectroscopy has | + | The size of proteins that can be studied by solution NMR spectroscopy has increased significantly because of recent developments in methodology. Important experiments include those that make use of approaches that increase the lifetimes of NMR signals or that define the orientation of internuclear bond vectors with respect to a common molecular frame. The advances in NMR techniques are strongly coupled to isotope labeling methods that increase sensitivity and reduce the complexity of NMR spectra. We show that these developments can be exploited in structural studies of high-molecular-weight, single-polypeptide proteins, and we present the solution global fold of the monomeric 723-residue (82-kDa) enzyme malate synthase G from Escherichia coli, which has been extensively characterized by NMR in the past several years. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y8B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9] Full crystallographic information is available from [http:// | + | 1Y8B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y8B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Malate synthase]] | [[Category: Malate synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Choy, W | + | [[Category: Choy, W Y.]] |
| - | [[Category: Kay, L | + | [[Category: Kay, L E.]] |
| - | [[Category: Orekhov, V | + | [[Category: Orekhov, V Y.]] |
[[Category: Tugarinov, V.]] | [[Category: Tugarinov, V.]] | ||
[[Category: 82 kda enzyme]] | [[Category: 82 kda enzyme]] | ||
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[[Category: nmr global fold]] | [[Category: nmr global fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:44 2008'' |
Revision as of 14:02, 21 February 2008
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Solution NMR-Derived Global Fold of Malate Synthase G from E.coli
Overview
The size of proteins that can be studied by solution NMR spectroscopy has increased significantly because of recent developments in methodology. Important experiments include those that make use of approaches that increase the lifetimes of NMR signals or that define the orientation of internuclear bond vectors with respect to a common molecular frame. The advances in NMR techniques are strongly coupled to isotope labeling methods that increase sensitivity and reduce the complexity of NMR spectra. We show that these developments can be exploited in structural studies of high-molecular-weight, single-polypeptide proteins, and we present the solution global fold of the monomeric 723-residue (82-kDa) enzyme malate synthase G from Escherichia coli, which has been extensively characterized by NMR in the past several years.
About this Structure
1Y8B is a Single protein structure of sequence from Escherichia coli. Active as Malate synthase, with EC number 2.3.3.9 Full crystallographic information is available from OCA.
Reference
Solution NMR-derived global fold of a monomeric 82-kDa enzyme., Tugarinov V, Choy WY, Orekhov VY, Kay LE, Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):622-7. Epub 2005 Jan 6. PMID:15637152
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