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PDBsum entry 1gh9
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Structural genomics, unknown function
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PDB id
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1gh9
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References listed in PDB file
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Key reference
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Title
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Structural proteomics of an archaeon.
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Authors
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D.Christendat,
A.Yee,
A.Dharamsi,
Y.Kluger,
A.Savchenko,
J.R.Cort,
V.Booth,
C.D.Mackereth,
V.Saridakis,
I.Ekiel,
G.Kozlov,
K.L.Maxwell,
N.Wu,
L.P.Mcintosh,
K.Gehring,
M.A.Kennedy,
A.R.Davidson,
E.F.Pai,
M.Gerstein,
A.M.Edwards,
C.H.Arrowsmith.
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Ref.
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Nat Struct Biol, 2000,
7,
903-909.
[DOI no: ]
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PubMed id
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Abstract
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A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were
cloned, expressed and purified for structural studies. Of these, approximately
20% were found to be suitable candidates for X-ray crystallographic or NMR
spectroscopic analysis without further optimization of conditions, providing an
estimate of the number of the most accessible structural targets in the
proteome. A retrospective analysis of the experimental behavior of these
proteins suggested some simple relations between sequence and solubility,
implying that data bases of protein properties will be useful in optimizing high
throughput strategies. Of the first 10 structures determined, several provided
clues to biochemical functions that were not detectable from sequence analysis,
and in many cases these putative functions could be readily confirmed by
biochemical methods. This demonstrates that structural proteomics is feasible
and can play a central role in functional genomics.
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Figure 1.
Figure 1. M.th. target ORFs. A histogram representing the
numbers of different classes of M.th. ORFs according to
predicted protein size showing unbiased sampling of nonmembrane
proteins of unknown structure.
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Figure 4.
Figure 4. Backbone ribbon representations of the first 10
protein structures.  -sheets
are shown in cyan and  -helices
in red. Bound cofactors and ligands are shown as ball-and-stick
models and metal ions as spheres. The M.th. gene number is given
along with the confirmed and/or putative (asterisks) biochemical
function of the protein. †Note that MTH150 is a homohexamer,
and MTH152 and MTH129 are homodimers, although only a single
subunit is displayed here.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2000,
7,
903-909)
copyright 2000.
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