1pj6
From Proteopedia
(New page: 200px<br /><applet load="1pj6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pj6, resolution 1.65Å" /> '''Crystal structure of...) |
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| - | [[Image:1pj6.jpg|left|200px]]<br /><applet load="1pj6" size=" | + | [[Image:1pj6.jpg|left|200px]]<br /><applet load="1pj6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pj6, resolution 1.65Å" /> | caption="1pj6, resolution 1.65Å" /> | ||
'''Crystal structure of dimethylglycine oxidase of Arthrobacter globiformis in complex with folic acid'''<br /> | '''Crystal structure of dimethylglycine oxidase of Arthrobacter globiformis in complex with folic acid'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Here we report crystal structures of dimethylglycine oxidase (DMGO) from | + | Here we report crystal structures of dimethylglycine oxidase (DMGO) from the bacterium Arthrobacter globiformis, a bifunctional enzyme that catalyzes the oxidation of N,N-dimethyl glycine and the formation of 5,10-methylene tetrahydrofolate. The N-terminal region binds FAD covalently and oxidizes dimethylglycine to a labile iminium intermediate. The C-terminal region binds tetrahydrofolate, comprises three domains arranged in a ring-like structure and is related to the T-protein of the glycine cleavage system. The complex with folinic acid indicates that this enzyme selectively activates the N10 amino group for initial attack on the substrate. Dead-end reactions with oxidized folate are avoided by the strict stereochemical constraints imposed by the folate-binding funnel. The active sites in DMGO are approximately 40 A apart, connected by a large irregular internal cavity. The tetrahydrofolate-binding funnel serves as a transient entry-exit port, and access to the internal cavity is controlled kinetically by tetrahydrofolate binding. The internal cavity enables sequestration of the reactive iminium intermediate prior to reaction with tetrahydrofolate and avoids formation of toxic formaldehyde. This mode of channelling in DMGO is distinct from other channelling mechanisms. |
==About this Structure== | ==About this Structure== | ||
| - | 1PJ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis] with NA, FOL and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dimethylglycine_oxidase Dimethylglycine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.10 1.5.3.10] Full crystallographic information is available from [http:// | + | 1PJ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=FOL:'>FOL</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dimethylglycine_oxidase Dimethylglycine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.10 1.5.3.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJ6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Basran, J.]] | [[Category: Basran, J.]] | ||
[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
| - | [[Category: Scrutton, N | + | [[Category: Scrutton, N S.]] |
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: FOL]] | [[Category: FOL]] | ||
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[[Category: folate binding]] | [[Category: folate binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:25 2008'' |
Revision as of 12:29, 21 February 2008
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Crystal structure of dimethylglycine oxidase of Arthrobacter globiformis in complex with folic acid
Overview
Here we report crystal structures of dimethylglycine oxidase (DMGO) from the bacterium Arthrobacter globiformis, a bifunctional enzyme that catalyzes the oxidation of N,N-dimethyl glycine and the formation of 5,10-methylene tetrahydrofolate. The N-terminal region binds FAD covalently and oxidizes dimethylglycine to a labile iminium intermediate. The C-terminal region binds tetrahydrofolate, comprises three domains arranged in a ring-like structure and is related to the T-protein of the glycine cleavage system. The complex with folinic acid indicates that this enzyme selectively activates the N10 amino group for initial attack on the substrate. Dead-end reactions with oxidized folate are avoided by the strict stereochemical constraints imposed by the folate-binding funnel. The active sites in DMGO are approximately 40 A apart, connected by a large irregular internal cavity. The tetrahydrofolate-binding funnel serves as a transient entry-exit port, and access to the internal cavity is controlled kinetically by tetrahydrofolate binding. The internal cavity enables sequestration of the reactive iminium intermediate prior to reaction with tetrahydrofolate and avoids formation of toxic formaldehyde. This mode of channelling in DMGO is distinct from other channelling mechanisms.
About this Structure
1PJ6 is a Single protein structure of sequence from Arthrobacter globiformis with , and as ligands. Active as Dimethylglycine oxidase, with EC number 1.5.3.10 Full crystallographic information is available from OCA.
Reference
Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase., Leys D, Basran J, Scrutton NS, EMBO J. 2003 Aug 15;22(16):4038-48. PMID:12912903
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