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PDBsum entry 6q4z
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PDB id:
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Transferase
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Title:
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Structure of an inactive variant (d94n) of mpt-2, a gdp-man-dependent mannosyltransferase from leishmania mexicana, in complex with beta-1, 2-mannobiose
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Structure:
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Lmxm mpt-2 d94n. Chain: a, b. Engineered: yes. Mutation: yes
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Source:
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Leishmania mexicana mhom/gt/2001/u1103. Organism_taxid: 929439. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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1.55Å
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R-factor:
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0.130
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R-free:
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0.189
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Authors:
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L.F.Sobala,A.Males,L.M.Bastidas,T.Ward,M.F.Sernee,J.E.Ralton, T.L.Nero,J.Kloehn,M.Viera-Lara,L.Stanton,S.Cobbold,D.E.Pires, E.Hanssen,M.W.Parker,D.B.Ascher,S.J.Williams,M.J.Mcconville, G.J.Davies
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Key ref:
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M.F.Sernee
et al.
(2019).
A Family of Dual-Activity Glycosyltransferase-Phosphorylases Mediates Mannogen Turnover and Virulence in Leishmania Parasites.
Cell Host Microbe,
26,
385.
PubMed id:
DOI:
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Date:
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06-Dec-18
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Release date:
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25-Sep-19
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PROCHECK
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Headers
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References
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E9AND8
(E9AND8_LEIMU) -
Glycosyl hydrolase-like protein from Leishmania mexicana (strain MHOM/GT/2001/U1103)
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Seq:
Struc:
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321 a.a.
310 a.a.*
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Key: |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Cell Host Microbe
26:385
(2019)
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PubMed id:
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A Family of Dual-Activity Glycosyltransferase-Phosphorylases Mediates Mannogen Turnover and Virulence in Leishmania Parasites.
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M.F.Sernee,
J.E.Ralton,
T.L.Nero,
L.F.Sobala,
J.Kloehn,
M.A.Vieira-Lara,
S.A.Cobbold,
L.Stanton,
D.E.V.Pires,
E.Hanssen,
A.Males,
T.Ward,
L.M.Bastidas,
P.L.van der Peet,
M.W.Parker,
D.B.Ascher,
S.J.Williams,
G.J.Davies,
M.J.McConville.
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ABSTRACT
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Parasitic protists belonging to the genus Leishmania synthesize the
non-canonical carbohydrate reserve, mannogen, which is composed of β-1,2-mannan
oligosaccharides. Here, we identify a class of
dual-activity mannosyltransferase/phosphorylases (MTPs) that catalyze both the
sugar nucleotide-dependent biosynthesis and phosphorolytic turnover of mannogen.
Structural and phylogenic analysis shows that while the MTPs are structurally
related to bacterial mannan phosphorylases, they constitute a distinct family of
glycosyltransferases (GT108) that have likely been acquired by horizontal gene
transfer from gram-positive bacteria. The seven MTPs catalyze the constitutive
synthesis and turnover of mannogen. This metabolic rheostat protects obligate
intracellular parasite stages from nutrient excess, and is essential for
thermotolerance and parasite infectivity in the mammalian host. Our results
suggest that the acquisition and expansion of the MTP family in Leishmania
increased the metabolic flexibility of these protists and contributed to their
capacity to colonize new host niches.
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Links
