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PDBsum entry 3mo4
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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The crystal structure of an alpha-(1-3,4)-fucosidase from bifidobacterium longum subsp. Infantis atcc 15697
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Structure:
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Alpha-1,3/4-fucosidase. Chain: a, b. Engineered: yes
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Source:
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Bifidobacterium longum subsp. Infantis. Organism_taxid: 391904. Strain: atcc 15697. Gene: blon_2336. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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1.90Å
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R-factor:
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0.164
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R-free:
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0.205
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Authors:
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K.Tan,X.Xu,H.Cui,J.Ng,A.Savchenko,A.Edwards,A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)
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Key ref:
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D.A.Sela
et al.
(2012).
Bifidobacterium longum subsp. infantis ATCC 15697 α-fucosidases are active on fucosylated human milk oligosaccharides.
Appl Environ Microbiol,
78,
795-803.
PubMed id:
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Date:
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22-Apr-10
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Release date:
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12-May-10
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PROCHECK
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Headers
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References
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B7GNN8
(B7GNN8_BIFLS) -
Alpha-1,3/4-fucosidase, putative from Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
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Seq:
Struc:
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478 a.a.
455 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Appl Environ Microbiol
78:795-803
(2012)
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PubMed id:
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Bifidobacterium longum subsp. infantis ATCC 15697 α-fucosidases are active on fucosylated human milk oligosaccharides.
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D.A.Sela,
D.Garrido,
L.Lerno,
S.Wu,
K.Tan,
H.J.Eom,
A.Joachimiak,
C.B.Lebrilla,
D.A.Mills.
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ABSTRACT
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Bifidobacterium longum subsp. infantis ATCC 15697 utilizes several small-mass
neutral human milk oligosaccharides (HMOs), several of which are fucosylated.
Whereas previous studies focused on endpoint consumption, a temporal glycan
consumption profile revealed a time-dependent effect. Specifically, among
preferred HMOs, tetraose was favored early in fermentation, with other
oligosaccharides consumed slightly later. In order to utilize fucosylated
oligosaccharides, ATCC 15697 possesses several fucosidases, implicating GH29 and
GH95 α-L-fucosidases in a gene cluster dedicated to HMO metabolism. Evaluation
of the biochemical kinetics demonstrated that ATCC 15697 expresses three
fucosidases with a high turnover rate. Moreover, several ATCC 15697 fucosidases
are active on the linkages inherent to the HMO molecule. Finally, the HMO
cluster GH29 α-L-fucosidase possesses a crystal structure that is similar to
previously characterized fucosidases.
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Links
