1wb6: Difference between revisions

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==Overview==

Feruloyl esterases play a key role in the degradation of the intricate, structure of the plant cell wall by hydrolysing the ferulate ester groups, involved in the cross-linking between hemicelluloses and between, hemicellulose and lignin. The structure of the feruloyl esterase module of, Clostridium thermocellum cellulosomal xylanase 10B has been reported, previously. It displays the alpha/beta hydrolase fold with a classical, Ser-His-Asp catalytic triad. Here, the structures of a Ser-Ala mutant of, this feruloyl esterase in complexes with methyl syringate, methyl, sinapinate and methyl vanillate are described. Substrate binding is, accompanied by subtle conformational changes at amino acids Trp982, Met955, Asn1023 and Ile1019 in the ligand-binding cavity. The structural, determinants, particularly the m-methoxy substituent, governing the, substrate specificity of Xyn10B feruloyl esterase are rationalized.

Feruloyl esterases play a key role in the degradation of the intricate structure of the plant cell wall by hydrolysing the ferulate ester groups involved in the cross-linking between hemicelluloses and between hemicellulose and lignin. The structure of the feruloyl esterase module of Clostridium thermocellum cellulosomal xylanase 10B has been reported previously. It displays the alpha/beta hydrolase fold with a classical Ser-His-Asp catalytic triad. Here, the structures of a Ser-Ala mutant of this feruloyl esterase in complexes with methyl syringate, methyl sinapinate and methyl vanillate are described. Substrate binding is accompanied by subtle conformational changes at amino acids Trp982, Met955, Asn1023 and Ile1019 in the ligand-binding cavity. The structural determinants, particularly the m-methoxy substituent, governing the substrate specificity of Xyn10B feruloyl esterase are rationalized.

==About this Structure==

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[[Category: Endo-1,4-beta-xylanase]]

[[Category: Single protein]]

[[Category: Davies, G.J.]]

[[Category: Davies, G J.]]

[[Category: Fontes, C.]]

[[Category: Prates, J.A.]]

[[Category: Prates, J A.]]

[[Category: Tarbouriech, N.]]

[[Category: ACT]]

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[[Category: xylanase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Feruloyl esterases play a key role in the degradation of the intricate, structure of the plant cell wall by hydrolysing the ferulate ester groups, involved in the cross-linking between hemicelluloses and between, hemicellulose and lignin. The structure of the feruloyl esterase module of, Clostridium thermocellum cellulosomal xylanase 10B has been reported, previously. It displays the alpha/beta hydrolase fold with a classical, Ser-His-Asp catalytic triad. Here, the structures of a Ser-Ala mutant of, this feruloyl esterase in complexes with methyl syringate, methyl, sinapinate and methyl vanillate are described. Substrate binding is, accompanied by subtle conformational changes at amino acids Trp982, Met955, Asn1023 and Ile1019 in the ligand-binding cavity. The structural, determinants, particularly the m-methoxy substituent, governing the, substrate specificity of Xyn10B feruloyl esterase are rationalized.
+Feruloyl esterases play a key role in the degradation of the intricate structure of the plant cell wall by hydrolysing the ferulate ester groups involved in the cross-linking between hemicelluloses and between hemicellulose and lignin. The structure of the feruloyl esterase module of Clostridium thermocellum cellulosomal xylanase 10B has been reported previously. It displays the alpha/beta hydrolase fold with a classical Ser-His-Asp catalytic triad. Here, the structures of a Ser-Ala mutant of this feruloyl esterase in complexes with methyl syringate, methyl sinapinate and methyl vanillate are described. Substrate binding is accompanied by subtle conformational changes at amino acids Trp982, Met955, Asn1023 and Ile1019 in the ligand-binding cavity. The structural determinants, particularly the m-methoxy substituent, governing the substrate specificity of Xyn10B feruloyl esterase are rationalized.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Endo-1,4-beta-xylanase]]
 [[Category: Single protein]]
-[[Category: Davies, G.J.]]
+[[Category: Davies, G J.]]
 [[Category: Fontes, C.]]
-[[Category: Prates, J.A.]]
+[[Category: Prates, J A.]]
 [[Category: Tarbouriech, N.]]
 [[Category: ACT]]
@@ Line 30: / Line 30: @@
 [[Category: xylanase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:21:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:24 2008''