1f52: Difference between revisions
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New page: left|200px<br /><applet load="1f52" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f52, resolution 2.49Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1f52.gif|left|200px]]<br /><applet load="1f52" size=" | [[Image:1f52.gif|left|200px]]<br /><applet load="1f52" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1f52, resolution 2.49Å" /> | caption="1f52, resolution 2.49Å" /> | ||
'''CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP'''<br /> | '''CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP'''<br /> | ||
==Overview== | ==Overview== | ||
Phosphinothricin is a potent inhibitor of the enzyme glutamine synthetase | Phosphinothricin is a potent inhibitor of the enzyme glutamine synthetase (GS). The resolution of the native structure of GS from Salmonella typhimurium has been extended to 2.5 A resolution, and the improved model is used to determine the structure of phosphinothricin complexed to GS by difference Fourier methods. The structure suggests a noncovalent, dead-end mechanism of inhibition. Phosphinothricin occupies the glutamate substrate pocket and stabilizes the Glu327 flap in a position which blocks the glutamate entrance to the active site, trapping the inhibitor on the enzyme. One oxygen of the phosphinyl group of phosphinothricin appears to be protonated, because of its proximity to the carboxylate group of Glu327. The other phosphinyl oxygen protrudes into the negatively charged binding pocket for the substrate ammonium, disrupting that pocket. The distribution of charges in the glutamate binding pocket is complementary to those of phosphinothricin. The presence of a second ammonium binding site within the active site is confirmed by its analogue thallous ion, marking the ammonium site and its protein ligands. The inhibition of GS by methionine sulfoximine can be explained by the same mechanism. These models of inhibited GS further illuminate its catalytic mechanism. | ||
==About this Structure== | ==About this Structure== | ||
1F52 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with MN, ADP and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Full crystallographic information is available from [http:// | 1F52 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F52 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: Gill, H | [[Category: Gill, H S.]] | ||
[[Category: Pfluegl, G | [[Category: Pfluegl, G M.U.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: mpd]] | [[Category: mpd]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:56 2008'' | ||
