2q0q
From Proteopedia
(New page: 200px<br /><applet load="2q0q" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q0q, resolution 1.50Å" /> '''Structure of the Nat...) |
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==Overview== | ==Overview== | ||
| - | The unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium | + | The unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium smegmatis forms the mechanistic basis for favoring alcoholysis over hydrolysis in water. Unlike hydrolases that perform alcoholysis only under anhydrous conditions, MsAcT demonstrates alcoholysis in substantially aqueous media and, in the presence of hydrogen peroxide, has a perhydrolysis:hydrolysis ratio 50-fold greater than that of the best lipase tested. The crystal structures of the apoenzyme and an inhibitor-bound form have been determined to 1.5 A resolution. MsAcT is an octamer in the asymmetric unit and forms a tightly associated aggregate in solution. Relative to other structurally similar monomers, MsAcT contains several insertions that contribute to the oligomerization and greatly restrict the shape of the active site, thereby limiting its accessibility. These properties create an environment by which MsAcT can catalyze transesterification reactions in an aqueous medium and suggests how a serine hydrolase can be engineered to be an efficient acyltransferase. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bott, R.]] | [[Category: Bott, R.]] | ||
| - | [[Category: Cervin, M | + | [[Category: Cervin, M A.]] |
[[Category: Ganshaw, G.]] | [[Category: Ganshaw, G.]] | ||
| - | [[Category: Mathews, I | + | [[Category: Mathews, I I.]] |
[[Category: Sala, R.]] | [[Category: Sala, R.]] | ||
[[Category: Saldajeno, M.]] | [[Category: Saldajeno, M.]] | ||
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[[Category: sgnh hydrolase]] | [[Category: sgnh hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:52 2008'' |
Revision as of 16:34, 21 February 2008
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Structure of the Native M. Smegmatis Aryl Esterase
Overview
The unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium smegmatis forms the mechanistic basis for favoring alcoholysis over hydrolysis in water. Unlike hydrolases that perform alcoholysis only under anhydrous conditions, MsAcT demonstrates alcoholysis in substantially aqueous media and, in the presence of hydrogen peroxide, has a perhydrolysis:hydrolysis ratio 50-fold greater than that of the best lipase tested. The crystal structures of the apoenzyme and an inhibitor-bound form have been determined to 1.5 A resolution. MsAcT is an octamer in the asymmetric unit and forms a tightly associated aggregate in solution. Relative to other structurally similar monomers, MsAcT contains several insertions that contribute to the oligomerization and greatly restrict the shape of the active site, thereby limiting its accessibility. These properties create an environment by which MsAcT can catalyze transesterification reactions in an aqueous medium and suggests how a serine hydrolase can be engineered to be an efficient acyltransferase.
About this Structure
2Q0Q is a Single protein structure of sequence from Mycobacterium smegmatis with and as ligands. Active as Arylesterase, with EC number 3.1.1.2 Full crystallographic information is available from OCA.
Reference
Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions., Mathews I, Soltis M, Saldajeno M, Ganshaw G, Sala R, Weyler W, Cervin MA, Whited G, Bott R, Biochemistry. 2007 Aug 7;46(31):8969-79. Epub 2007 Jul 18. PMID:17636869
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