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PDBsum entry 2khr
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Biosynthetic protein
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PDB id
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2khr
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References listed in PDB file
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Key reference
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Title
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Solution structure of rv2377c-Founding member of the mbth-Like protein family.
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Authors
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G.W.Buchko,
C.Y.Kim,
T.C.Terwilliger,
P.J.Myler.
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Ref.
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Tuberculosis (edinb), 2010,
90,
245-251.
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PubMed id
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Abstract
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The Mycobacterium tuberculosis protein Rv2377c (71 residues, MW=8.4kDa) has been
characterized using nuclear magnetic resonance (NMR) and circular dichroism (CD)
spectroscopy. Rv2377c was the first identified member of the MbtH-like family of
proteins. MbtH-like proteins have been implicated in siderophore biosynthesis,
however, their precise biochemical function remain unknown. Size exclusion
chromatography and NMR spectroscopy show that Rv2377c is a monomer in solution.
Circular dichroism spectroscopy indicates that Rv2377c unfolds upon heating and
will reversibly fold into its native conformation upon cooling. Using NMR-based
methods the solution structure of Rv2377c was determined and some of the dynamic
properties of the protein studied. The protein contains a three-strand,
anti-parallel beta-sheet (beta3:beta1:beta2) nestled against one C-terminal
alpha-helix (S44-N55). Weak or absent amide cross peaks in the (1)H-(15)N HSQC
spectrum for many of the beta1 and beta2 residues suggest intermediate motion on
the ms to mus time scale at the beta1:beta2 interface. Amide cross peaks in the
(1)H-(15)N HSQC spectrum are absent for all but one residue at the C-terminus
(W56-D71), a region that includes a highly conserved sequence WXDXR, suggesting
this region is intrinsically disordered. The latter observation differs with the
crystal structure of another MbtH-like protein, PA2412 from Pseudomonas
aeruginosa, where a second ordered alpha-helix was observed at the extreme
C-terminus.
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