Structural analysis of glucuronoxylan-specific Xyn30D and its attached CBM35 domain gives insights into the role of modularity in specificity (Q42118132)

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scientific article published on 8 September 2014

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English	Structural analysis of glucuronoxylan-specific Xyn30D and its attached CBM35 domain gives insights into the role of modularity in specificity	scientific article published on 8 September 2014

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16 February 2020

Structural analysis of glucuronoxylan-specific Xyn30D and its attached CBM35 domain gives insights into the role of modularity in specificity (English)

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16 February 2020

Susana V Valenzuela

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16 February 2020

Beatriz González

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16 February 2020

Francisco I. Pastor

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16 February 2020

Julia Sanz-Aparicio

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16 February 2020

M Angela Sainz-Polo

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M Angela Sainz-Polo

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8 September 2014

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16 February 2020

Journal of Biological Chemistry

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16 February 2020

289

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16 February 2020

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16 February 2020

31088-31101

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16 February 2020

Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis.

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Recent advances in understanding the role of cellulose accessibility in enzymatic hydrolysis of lignocellulosic substrates.

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The carbohydrate-active enzymes database (CAZy) in 2013

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Modular glucuronoxylan-specific xylanase with a family CBM35 carbohydrate-binding module.

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Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase

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Overview of the CCP4 suite and current developments

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Ligand bound structures of a glycosyl hydrolase family 30 glucuronoxylan xylanohydrolase

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Consolidation of glycosyl hydrolase family 30: a dual domain 4/7 hydrolase family consisting of two structurally distinct groups

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Signature active site architectures illuminate the molecular basis for ligand specificity in family 35 carbohydrate binding module

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16 February 2020

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