1mtc: Difference between revisions
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New page: left|200px<br /><applet load="1mtc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mtc, resolution 2.20Å" /> '''GLUTATHIONE TRANSFER... |
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[[Image:1mtc.jpg|left|200px]]<br /><applet load="1mtc" size=" | [[Image:1mtc.jpg|left|200px]]<br /><applet load="1mtc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1mtc, resolution 2.20Å" /> | caption="1mtc, resolution 2.20Å" /> | ||
'''GLUTATHIONE TRANSFERASE MUTANT Y115F'''<br /> | '''GLUTATHIONE TRANSFERASE MUTANT Y115F'''<br /> | ||
==Overview== | ==Overview== | ||
Glutathione transferase rGSTM1-1 catalyzes the addition of glutathione | Glutathione transferase rGSTM1-1 catalyzes the addition of glutathione (GSH) to 1-chloro-2,4-dinitrobenzene, a reaction in which the chemical step is 60-fold faster than the physical step of product release. The hydroxyl group of Y115, located in the active site access channel, controls the egress of product from the active site. The Y115F mutant enzyme has a k(cat) (72 s(-)(1)) that is 3.6-fold larger than that of the native enzyme (20 s(-)(1)). Crystallographic observations and evidence from amide proton exchange kinetics are consistent with localized increases in the degree of segmental motion of the Y115F mutant that are coupled to the enhanced rate of product release. The loss of hydrogen bonding interactions involving the hydroxyl group of Y115 is reflected in subtle alterations in the backbone position, an increase in B-factors for structural elements that comprise the channel to the active site, and, most dramatically, a loss of well-defined electron density near the site of mutation. The kinetics of amide proton exchange are also enhanced by a factor between 3 and 12 in these regions, providing direct, quantitative evidence for changes in local protein dynamics affecting product release. The enhanced product release rate is proposed to derive from a small shift in the equilibrium population of protein conformers that permit egress of the product from the active site. | ||
==About this Structure== | ==About this Structure== | ||
1MTC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GPR as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http:// | 1MTC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=GPR:'>GPR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Armstrong, R | [[Category: Armstrong, R N.]] | ||
[[Category: Gilliland, G | [[Category: Gilliland, G L.]] | ||
[[Category: Ladner, J | [[Category: Ladner, J E.]] | ||
[[Category: Xiao, G.]] | [[Category: Xiao, G.]] | ||
[[Category: GPR]] | [[Category: GPR]] | ||
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[[Category: protein dynamics]] | [[Category: protein dynamics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:47 2008'' | ||