2axr

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(New page: 200px<br /><applet load="2axr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2axr, resolution 1.980&Aring;" /> '''Crystal structure o...)
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==Overview==
==Overview==
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Glucooligosaccharide oxidase from Acremonium strictum has been screened, for potential applications in oligosaccharide acid production and, alternative carbohydrate detection, because it catalyzes the oxidation of, glucose, maltose, lactose, cellobiose and cello- and, maltooligosaccharides. We report the crystal structures of the enzyme and, of its complex with an inhibitor, 5-amino-5-deoxy- cellobiono-1,5-lactam, at 1.55- and 1.98-A resolution, respectively. Unexpectedly, the protein, structure demonstrates the first known double attachment flavinylation, 6-S-cysteinyl, 8alpha-N1-histidyl FAD. The FAD cofactor is cross-linked to, the enzyme via the C(6) atom and the 8alpha-methyl group of the, isoalloxazine ring with Cys(130) and His(70), respectively. This sugar, oxidase possesses an open carbohydrate-binding groove, allowing the, accommodation of higher oligosaccharides. The complex structure suggests, that this enzyme may prefer a beta-d-glucosyl residue at the reducing end, with the conserved Tyr(429) acting as a general base to abstract the OH(1), proton in concert with the H(1) hydride transfer to the flavin N(5)., Finally, a detailed comparison illustrates the structural conservation as, well as the divergence between this protein and its related flavoenzymes.
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Glucooligosaccharide oxidase from Acremonium strictum has been screened for potential applications in oligosaccharide acid production and alternative carbohydrate detection, because it catalyzes the oxidation of glucose, maltose, lactose, cellobiose and cello- and maltooligosaccharides. We report the crystal structures of the enzyme and of its complex with an inhibitor, 5-amino-5-deoxy- cellobiono-1,5-lactam at 1.55- and 1.98-A resolution, respectively. Unexpectedly, the protein structure demonstrates the first known double attachment flavinylation, 6-S-cysteinyl, 8alpha-N1-histidyl FAD. The FAD cofactor is cross-linked to the enzyme via the C(6) atom and the 8alpha-methyl group of the isoalloxazine ring with Cys(130) and His(70), respectively. This sugar oxidase possesses an open carbohydrate-binding groove, allowing the accommodation of higher oligosaccharides. The complex structure suggests that this enzyme may prefer a beta-d-glucosyl residue at the reducing end with the conserved Tyr(429) acting as a general base to abstract the OH(1) proton in concert with the H(1) hydride transfer to the flavin N(5). Finally, a detailed comparison illustrates the structural conservation as well as the divergence between this protein and its related flavoenzymes.
==About this Structure==
==About this Structure==
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[[Category: Acremonium strictum]]
[[Category: Acremonium strictum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Huang, C.H.]]
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[[Category: Huang, C H.]]
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[[Category: Lai, W.L.]]
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[[Category: Lai, W L.]]
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[[Category: Liaw, S.H.]]
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[[Category: Liaw, S H.]]
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[[Category: Tsai, Y.C.]]
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[[Category: Tsai, Y C.]]
[[Category: Vasella, A.]]
[[Category: Vasella, A.]]
[[Category: ABL]]
[[Category: ABL]]
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[[Category: covalent flavoenzyme]]
[[Category: covalent flavoenzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:12:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:07 2008''

Revision as of 14:32, 21 February 2008

Image:2axr.gif

2axr, resolution 1.980Å

Drag the structure with the mouse to rotate

Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD

Overview

Glucooligosaccharide oxidase from Acremonium strictum has been screened for potential applications in oligosaccharide acid production and alternative carbohydrate detection, because it catalyzes the oxidation of glucose, maltose, lactose, cellobiose and cello- and maltooligosaccharides. We report the crystal structures of the enzyme and of its complex with an inhibitor, 5-amino-5-deoxy- cellobiono-1,5-lactam at 1.55- and 1.98-A resolution, respectively. Unexpectedly, the protein structure demonstrates the first known double attachment flavinylation, 6-S-cysteinyl, 8alpha-N1-histidyl FAD. The FAD cofactor is cross-linked to the enzyme via the C(6) atom and the 8alpha-methyl group of the isoalloxazine ring with Cys(130) and His(70), respectively. This sugar oxidase possesses an open carbohydrate-binding groove, allowing the accommodation of higher oligosaccharides. The complex structure suggests that this enzyme may prefer a beta-d-glucosyl residue at the reducing end with the conserved Tyr(429) acting as a general base to abstract the OH(1) proton in concert with the H(1) hydride transfer to the flavin N(5). Finally, a detailed comparison illustrates the structural conservation as well as the divergence between this protein and its related flavoenzymes.

About this Structure

2AXR is a Single protein structure of sequence from Acremonium strictum with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD., Huang CH, Lai WL, Lee MH, Chen CJ, Vasella A, Tsai YC, Liaw SH, J Biol Chem. 2005 Nov 18;280(46):38831-8. Epub 2005 Sep 9. PMID:16154992

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