1uwc: Difference between revisions

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==Overview==
==Overview==
The crystallographic structure of feruloyl esterase from Aspergillus niger, has been determined to a resolution of 1.5 A by molecular replacement. The, protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic, triad; the overall fold of the protein is very similar to that of the, fungal lipases. The structure of the enzyme-product complex was determined, to a resolution of 1.08 A and reveals dual conformations for the serine, and histidine residues at the active site.
The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site.


==About this Structure==
==About this Structure==
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[[Category: Feruloyl esterase]]
[[Category: Feruloyl esterase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mcauley, K.E.]]
[[Category: Mcauley, K E.]]
[[Category: Patkar, S.A.]]
[[Category: Patkar, S A.]]
[[Category: Svendsen, A.]]
[[Category: Svendsen, A.]]
[[Category: Wilson, K.S.]]
[[Category: Wilson, K S.]]
[[Category: FER]]
[[Category: FER]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: xylan degradation]]
[[Category: xylan degradation]]


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