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PDBsum entry 6en3
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PDB id:
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Hydrolase
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Title:
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Crystal structure of full length endos from streptococcus pyogenes in complex with g2 oligosaccharide.
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Structure:
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Endo-beta-n-acetylglucosaminidase f2,multifunctional- autoprocessing repeats-in-toxin. Chain: a. Synonym: martx. Engineered: yes. Mutation: yes
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Source:
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Streptococcus pyogenes, vibrio cholerae. Organism_taxid: 1314, 666. Gene: endos, m1gas476_1618, rtxa, rtx, vc_1451. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.90Å
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R-factor:
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0.211
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R-free:
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0.240
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Authors:
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B.Trastoy,E.H.Klontz,J.Orwenyo,A.Marina,L.X.Wang,E.J.Sundberg, M.E.Guerin
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Key ref:
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B.Trastoy
et al.
(2018).
Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S.
Nat Commun,
9,
1874.
PubMed id:
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Date:
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04-Oct-17
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Release date:
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13-Jun-18
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PROCHECK
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Headers
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References
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Q9KS12
(MARTX_VIBCH) -
Multifunctional-autoprocessing repeats-in-toxin from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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Seq:
Struc:
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4558 a.a.
934 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 823 residue positions (black
crosses)
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Enzyme class 2:
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E.C.2.3.1.-
- ?????
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Enzyme class 3:
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E.C.3.4.22.-
- ?????
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Enzyme class 4:
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E.C.6.3.2.-
- ?????
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Nat Commun
9:1874
(2018)
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PubMed id:
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Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S.
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B.Trastoy,
E.Klontz,
J.Orwenyo,
A.Marina,
L.X.Wang,
E.J.Sundberg,
M.E.Guerin.
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ABSTRACT
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Endoglycosidase S (EndoS) is a bacterial endo-β-N-acetylglucosaminidase that
specifically catalyzes the hydrolysis of the β-1,4 linkage between the first
two N-acetylglucosamine residues of the biantennary complex-type N-linked
glycans of IgG Fc regions. It is used for the chemoenzymatic synthesis of
homogeneously glycosylated antibodies with improved therapeutic properties, but
the molecular basis for its substrate specificity is unknown. Here, we report
the crystal structure of the full-length EndoS in complex with its
oligosaccharide G2 product. The glycoside hydrolase domain contains two
well-defined asymmetric grooves that accommodate the complex-type N-linked
glycan antennae near the active site. Several loops shape the glycan binding
site, thereby governing the strict substrate specificity of EndoS. Comparing the
arrangement of these loops within EndoS and related endoglycosidases, reveals
distinct-binding site architectures that correlate with the respective glycan
specificities, providing a basis for the bioengineering of endoglycosidases to
tailor the chemoenzymatic synthesis of monoclonal antibodies.
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