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PDBsum entry 4zra
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Lipid binding protein
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PDB id
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4zra
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PDB id:
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| Name: |
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Lipid binding protein
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Title:
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Crystal structure of mycobacterium tuberculosis lprg binding to triacylglyceride
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Structure:
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Lipoprotein lprg. Chain: a, c. Synonym: 27 kda lipoprotein,antigen p27. Engineered: yes
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Source:
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Mycobacterium tuberculosis (strain atcc 25618 / h37rv). Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: lprg, lpp-27, rv1411c, mtcy21b4.28c. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.83Å
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R-factor:
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0.205
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R-free:
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0.234
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Authors:
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A.J.Martinot,M.Farrow,L.Bai,E.Layre,T.Y.Cheng,J.H.C.Tsai,J.Iqbal, J.Annand,Z.Sullivan,M.Hussain,J.Sacchettini,D.B.Moody,J.Seeliger, E.J.Rubin,Tb Structural Genomics Consortium (Tbsgc)
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Key ref:
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A.J.Martinot
et al.
(2016).
Mycobacterial Metabolic Syndrome: LprG and Rv1410 Regulate Triacylglyceride Levels, Growth Rate and Virulence in Mycobacterium tuberculosis.
Plos Pathog,
12,
e1005351.
PubMed id:
DOI:
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Date:
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12-May-15
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Release date:
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10-Feb-16
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PROCHECK
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Headers
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References
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P9WK45
(LPRG_MYCTU) -
Lipoarabinomannan carrier protein LprG from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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Seq:
Struc:
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236 a.a.
196 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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DOI no:
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Plos Pathog
12:e1005351
(2016)
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PubMed id:
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Mycobacterial Metabolic Syndrome: LprG and Rv1410 Regulate Triacylglyceride Levels, Growth Rate and Virulence in Mycobacterium tuberculosis.
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A.J.Martinot,
M.Farrow,
L.Bai,
E.Layre,
T.Y.Cheng,
J.H.Tsai,
J.Iqbal,
J.W.Annand,
Z.A.Sullivan,
M.M.Hussain,
J.Sacchettini,
D.B.Moody,
J.C.Seeliger,
E.J.Rubin.
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ABSTRACT
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Mycobacterium tuberculosis (Mtb) mutants lacking rv1411c, which encodes the
lipoprotein LprG, and rv1410c, which encodes a putative efflux pump, are
dramatically attenuated for growth in mice. Here we show that loss of
LprG-Rv1410 in Mtb leads to intracellular triacylglyceride (TAG) accumulation,
and overexpression of the locus increases the levels of TAG in the culture
medium, demonstrating a role of this locus in TAG transport. LprG binds TAG
within a large hydrophobic cleft and is sufficient to transfer TAG from donor to
acceptor membranes. Further, LprG-Rv1410 is critical for broadly regulating
bacterial growth and metabolism in vitro during carbon restriction and in vivo
during infection of mice. The growth defect in mice is due to disrupted
bacterial metabolism and occurs independently of key immune regulators. The in
vivo essentiality of this locus suggests that this export system and other
regulators of metabolism should be considered as targets for novel therapeutics.
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Links
