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| {{STRUCTURE_1wb6| PDB=1wb6 | SCENE= }} | | {{STRUCTURE_1wb6| PDB=1wb6 | SCENE= }} |
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| '''S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH VANILLATE'''
| | ===S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH VANILLATE=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15681871}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15681871 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15681871}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Xylan degradation]] | | [[Category: Xylan degradation]] |
| [[Category: Xylanase]] | | [[Category: Xylanase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:24:34 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:47:19 2008'' |