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PDBsum entry 6rv8
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PDB id:
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Hydrolase
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Title:
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Crystal structure of glucuronoyl esterase from cerrena unicolor covalent complex with the aldouronic acid uxxr
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Structure:
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4-o-methyl-glucuronoyl methylesterase. Chain: a, b. Synonym: glucuronoyl esterase,ge. Engineered: yes
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Source:
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Cerrena unicolor. Organism_taxid: 90312. Expressed in: komagataella pastoris. Expression_system_taxid: 4922. Expression_system_variant: x-33.
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Resolution:
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1.85Å
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R-factor:
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0.151
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R-free:
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0.181
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Authors:
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H.A.Ernst,C.Mosbech,A.Langkilde,P.Westh,A.Meyer,J.W.Agger,S.Larsen
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Key ref:
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H.A.Ernst
et al.
(2020).
The structural basis of fungal glucuronoyl esterase activity on natural substrates.
Nat Commun,
11,
1026.
PubMed id:
DOI:
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Date:
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31-May-19
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Release date:
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18-Mar-20
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PROCHECK
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Headers
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References
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A0A0A7EQR3
(GCE_CERUI) -
4-O-methyl-glucuronoyl methylesterase from Cerrena unicolor
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Seq:
Struc:
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474 a.a.
381 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.3.1.1.117
- (4-O-methyl)-D-glucuronate--lignin esterase.
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Reaction:
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a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl- alpha-D-glucuronate derivative + an alcohol + H+
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4-O-methyl-alpha-D-glucuronosyl ester derivative
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+
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H2O
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=
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4-O-methyl- alpha-D-glucuronate derivative
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+
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alcohol
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Nat Commun
11:1026
(2020)
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PubMed id:
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The structural basis of fungal glucuronoyl esterase activity on natural substrates.
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H.A.Ernst,
C.Mosbech,
A.E.Langkilde,
P.Westh,
A.S.Meyer,
J.W.Agger,
S.Larsen.
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ABSTRACT
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Structural and functional studies were conducted of the glucuronoyl esterase
(GE) from Cerrena unicolor (CuGE), an enzyme catalyzing cleavage of
lignin-carbohydrate ester bonds. CuGE is an α/β-hydrolase belonging to
carbohydrate esterase family 15 (CE15). The enzyme is modular, comprised of a
catalytic and a carbohydrate-binding domain. SAXS data show CuGE as an elongated
rigid molecule where the two domains are connected by a rigid linker. Detailed
structural information of the catalytic domain in its apo- and inactivated form
and complexes with aldouronic acids reveal well-defined binding of the
4-O-methyl-a-D-glucuronoyl moiety, not influenced by the nature of the attached
xylo-oligosaccharide. Structural and sequence comparisons within CE15 enzymes
reveal two distinct structural subgroups. CuGE belongs to the group of fungal
CE15-B enzymes with an open and flat substrate-binding site. The interactions
between CuGE and its natural substrates are explained and rationalized by the
structural results, microscale thermophoresis and isothermal calorimetry.
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