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PDBsum entry 4xrr
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Oxidoreductase
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PDB id
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4xrr
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Crystal structure of cals8 from micromonospora echinospora (p294s mutant)
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Structure:
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Cals8. Chain: a, b. Engineered: yes. Mutation: yes
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Source:
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Micromonospora echinospora. Organism_taxid: 1877. Gene: cals8. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.55Å
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R-factor:
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0.185
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R-free:
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0.225
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Authors:
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K.Michalska,L.Bigelow,M.Endres,G.Babnigg,C.A.Bingman,R.M.Yennamalli, S.Singh,M.K.Kharel,J.S.Thorson,G.N.Phillips Jr.,A.Joachimiak,Midwest Center For Structural Genomics (Mcsg),Enzyme Discovery For Natural Product Biosynthesis (Natpro)
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Key ref:
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S.Singh
et al.
(2015).
Structural Characterization of CalS8, a TDP-α-D-Glucose Dehydrogenase Involved in Calicheamicin Aminodideoxypentose Biosynthesis.
J Biol Chem,
290,
26249-26258.
PubMed id:
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Date:
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21-Jan-15
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Release date:
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11-Feb-15
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Supersedes:
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PROCHECK
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Headers
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References
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Q8KNF6
(Q8KNF6_MICEC) -
CalS8 from Micromonospora echinospora
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Seq:
Struc:
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453 a.a.
453 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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J Biol Chem
290:26249-26258
(2015)
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PubMed id:
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Structural Characterization of CalS8, a TDP-α-D-Glucose Dehydrogenase Involved in Calicheamicin Aminodideoxypentose Biosynthesis.
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S.Singh,
K.Michalska,
L.Bigelow,
M.Endres,
M.K.Kharel,
G.Babnigg,
R.M.Yennamalli,
C.A.Bingman,
A.Joachimiak,
J.S.Thorson,
G.N.Phillips.
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ABSTRACT
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Classical UDP-glucose 6-dehydrogenases (UGDHs; EC 1.1.1.22) catalyze the
conversion of UDP-α-d-glucose (UDP-Glc) to the key metabolic precursor
UDP-α-d-glucuronic acid (UDP-GlcA) and display specificity for UDP-Glc. The
fundamental biochemical and structural study of the UGDH homolog CalS8 encoded
by the calicheamicin biosynthetic gene is reported and represents one of the
first studies of a UGDH homolog involved in secondary metabolism. The
corresponding biochemical characterization of CalS8 reveals CalS8 as one of the
first characterized base-permissive UGDH homologs with a >15-fold preference
for TDP-Glc over UDP-Glc. The corresponding structure elucidations of apo-CalS8
and the CalS8·substrate·cofactor ternary complex (at 2.47 and 1.95 Å
resolution, respectively) highlight a notably high degree of conservation
between CalS8 and classical UGDHs where structural divergence within the
intersubunit loop structure likely contributes to the CalS8 base permissivity.
As such, this study begins to provide a putative blueprint for base specificity
among sugar nucleotide-dependent dehydrogenases and, in conjunction with prior
studies on the base specificity of the calicheamicin aminopentosyltransferase
CalG4, provides growing support for the calicheamicin aminopentose pathway as a
TDP-sugar-dependent process.
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