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PDBsum entry 1xhs
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Structural genomics, unknown function
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PDB id
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1xhs
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Contents |
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* Residue conservation analysis
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PDB id:
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Structural genomics, unknown function
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Title:
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Solution nmr structure of protein ytfp from escherichia coli. Northeast structural genomics consortium target er111.
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Structure:
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Hypothetical upf0131 protein ytfp. Chain: a. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: ytfp. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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10 models
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Authors:
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J.M.Aramini,Y.J.Huang,G.V.T.Swapna,R.K.Paranji,R.Xiao,R.Shastry, T.B.Acton,J.R.Cort,M.A.Kennedy,G.T.Montelione,Northeast Structural Genomics Consortium (Nesg)
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Key ref:
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J.M.Aramini
et al.
(2007).
Solution NMR structure of Escherichia coli ytfP expands the structural coverage of the UPF0131 protein domain family.
Proteins,
68,
789-795.
PubMed id:
DOI:
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Date:
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20-Sep-04
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Release date:
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04-Jan-05
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PROCHECK
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Headers
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References
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P0AE48
(YTFP_ECOLI) -
Gamma-glutamylcyclotransferase family protein YtfP from Escherichia coli (strain K12)
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Seq: Struc:
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113 a.a.
113 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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Proteins
68:789-795
(2007)
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PubMed id:
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Solution NMR structure of Escherichia coli ytfP expands the structural coverage of the UPF0131 protein domain family.
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J.M.Aramini,
Y.J.Huang,
G.V.Swapna,
J.R.Cort,
P.K.Rajan,
R.Xiao,
R.Shastry,
T.B.Acton,
J.Liu,
B.Rost,
M.A.Kennedy,
G.T.Montelione.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. (A) A subset of the multiple sequence alignment of
the entire UPF0131 protein domain family (Pfam release 20.0)
aligned using Clustal X.[4] Representatives from bacteria,
archaea, and eukaryotes, indicated by their Swiss-Prot IDs, are
listed in black, magenta, and green, respectively. Amino acid
residues identical or similar in 67% of the entire family are
shown in red and green, respectively; conserved residues were
colored using the BOXSHADE server. The sequence numbering for
yftP from E. coli and the secondary structural elements found in
its NMR structure described in this paper (1XHS) are shown above
the alignment. (B) Stereoview of the solution structure of ytfP
showing the backbone atom superposition of the final ensemble of
10 conformers representing the solution structure of ytfP; -strand
elements are shown in green, -helices
are in red. (C) Stereoview of the ribbon representation of a
representative conformer (lowest CNS energy) from the ensemble
generated using MOLMOL.[5] The secondary structural elements are
labeled.
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Figure 2.
Figure 2. (A) GRASP[29] electrostatic potential surfaces
showing the face of ytfP containing the positively charged
(blue) cavity (top) and the opposite face of the protein
(bottom). (B) Two ConSurf[30] images of ytfP based on the
multiple sequence alignment of the entire UPF0131 protein domain
family. Residue coloring, reflecting the degree of residue
conservation over the entire family, ranges from magenta (highly
conserved) to cyan (variable). (C) Ribbon diagrams of the
pairwise structural alignments of the solution structure of E.
coli ytfP (1XHS; residues 1-113), crystal structure of P.
horikoshii Y828_PYRHO (1V306; 7-116 plus C-terminal tag), and
crystal structure of M.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
68,
789-795)
copyright 2007.
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Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Sharma,
H.Zheng,
Y.J.Huang,
A.Ertekin,
Y.Hamuro,
P.Rossi,
R.Tejero,
T.B.Acton,
R.Xiao,
M.Jiang,
L.Zhao,
L.C.Ma,
G.V.Swapna,
J.M.Aramini,
and
G.T.Montelione
(2009).
Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry.
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Proteins,
76,
882-894.
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J.M.Aramini,
S.Sharma,
Y.J.Huang,
G.V.Swapna,
C.K.Ho,
K.Shetty,
K.Cunningham,
L.C.Ma,
L.Zhao,
L.A.Owens,
M.Jiang,
R.Xiao,
J.Liu,
M.C.Baran,
T.B.Acton,
B.Rost,
and
G.T.Montelione
(2008).
Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis.
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Proteins,
72,
526-530.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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