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PDBsum entry 1jw2
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Gene regulation
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PDB id
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1jw2
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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An nmr approach to structural proteomics.
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Authors
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A.Yee,
X.Chang,
A.Pineda-Lucena,
B.Wu,
A.Semesi,
B.Le,
T.Ramelot,
G.M.Lee,
S.Bhattacharyya,
P.Gutierrez,
A.Denisov,
C.H.Lee,
J.R.Cort,
G.Kozlov,
J.Liao,
G.Finak,
L.Chen,
D.Wishart,
W.Lee,
L.P.Mcintosh,
K.Gehring,
M.A.Kennedy,
A.M.Edwards,
C.H.Arrowsmith.
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Ref.
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Proc Natl Acad Sci U S A, 2002,
99,
1825-1830.
[DOI no: ]
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PubMed id
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Abstract
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The influx of genomic sequence information has led to the concept of structural
proteomics, the determination of protein structures on a genome-wide scale. Here
we describe an approach to structural proteomics of small proteins using NMR
spectroscopy. Over 500 small proteins from several organisms were cloned,
expressed, purified, and evaluated by NMR. Although there was variability among
proteomes, overall 20% of these proteins were found to be readily amenable to
NMR structure determination. NMR sample preparation was centralized in one
facility, and a distributive approach was used for NMR data collection and
analysis. Twelve structures are reported here as part of this approach, which
allowed us to infer putative functions for several conserved hypothetical
proteins.
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Figure 1.
Fig. 1. Histogram of the number of proteins cloned
(blue), expressed (red), and soluble (gray) from each organism.
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Figure 3.
Fig. 3. 15N HSQC spectra and the backbone ribbon
representations of the 12 structures presented in this paper.
All HSQCs are plotted from 6.0-10.5 ppm in the 1H dimension (x
axis) and from 107 to 133 ppm in the 15N dimension (y axis). The
number of residues for each protein is indicated on the HSQC
spectrum.  -sheets are
shown in cyan, and  -helices
are shown in red. N-terminal residues 1-20 of yedF_ecoli and
Myxv156r are unstructured and not shown. C-terminal residues
198-208 of Mth1692 are unstructured and not shown. All structure
diagrams were created by using the MOLAUTO program within
MOLSCRIPT (17).
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