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PDBsum entry 1nya
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Metal binding protein
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PDB id
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1nya
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Contents |
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* Residue conservation analysis
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DOI no:
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Eur J Biochem
270:2505-2512
(2003)
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PubMed id:
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NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.
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H.Tossavainen,
P.Permi,
A.Annila,
I.Kilpeläinen,
T.Drakenberg.
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ABSTRACT
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The structure of calerythrin, a prokaryotic 20 kDa calcium-binding protein has
been determined by solution NMR spectroscopy. Distance, dihedral angle, J
coupling, secondary chemical shift, residual dipolar coupling and radius of
gyration restraints reveal four EF-hand motifs arranged in a compact globular
structure. A tight turn in the middle of the amino acid sequence brings the two
halves, each comprising a pair of EF-hands, close together. The structural
similarity between calerythrin and the eukaryotic sarcoplasmic calcium-binding
proteins is notable.
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Selected figure(s)
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Figure 4.
Fig. 4. Ribbon representation of the refined lowest-energy
structure. EF-hands are represented by different colours, EF-1
yellow, EF-2 red, EF-3 green and EF-4 blue. The short -sheet is
represented by arrows. The kink between the halves can be seen
between helix D (red) and helix E (green). Calcium ions are
represented as orange spheres.
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Figure 5.
Fig. 5. A stereo view of calerythrin superimposed with
N-SCP. The colour code is the same as in Fig. 4 Go- .
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
Eur J Biochem
(2003,
270,
2505-2512)
copyright 2003.
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Figures were
selected
by an automated process.
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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.L.Wang,
K.Q.Fan,
X.Yang,
Z.X.Lin,
X.P.Xu,
and
K.Q.Yang
(2008).
CabC, an EF-hand calcium-binding protein, is involved in Ca2+-mediated regulation of spore germination and aerial hypha formation in Streptomyces coelicolor.
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J Bacteriol,
190,
4061-4068.
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X.Zhao,
S.Wang,
H.Pang,
K.Yang,
and
M.Bartlam
(2008).
Crystallization and preliminary X-ray diffraction studies of the calcium-binding protein CalD from Streptomyces coelicolor.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
816-818.
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M.Louhivuori,
R.Otten,
T.Salminen,
and
A.Annila
(2007).
Evidence of molecular alignment fluctuations in aqueous dilute liquid crystalline media.
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J Biomol NMR,
39,
141-152.
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U.Ryde
(2007).
Accurate metal-site structures in proteins obtained by combining experimental data and quantum chemistry.
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Dalton Trans,
(),
607-625.
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Y.Zhou,
W.Yang,
M.Kirberger,
H.W.Lee,
G.Ayalasomayajula,
and
J.J.Yang
(2006).
Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins.
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Proteins,
65,
643-655.
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G.Rabah,
R.Popescu,
J.A.Cox,
Y.Engelborghs,
and
C.T.Craescu
(2005).
Solution structure and internal dynamics of NSCP, a compact calcium-binding protein.
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FEBS J,
272,
2022-2036.
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PDB code:
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J.H.Prestegard,
K.L.Mayer,
H.Valafar,
and
G.C.Benison
(2005).
Determination of protein backbone structures from residual dipolar couplings.
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Methods Enzymol,
394,
175-209.
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Y.W.Hsiao,
T.Drakenberg,
and
U.Ryde
(2005).
NMR structure determination of proteins supplemented by quantum chemical calculations: detailed structure of the Ca2+ sites in the EGF34 fragment of protein S.
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J Biomol NMR,
31,
97.
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Y.Qu,
J.T.Guo,
V.Olman,
and
Y.Xu
(2004).
Protein structure prediction using sparse dipolar coupling data.
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Nucleic Acids Res,
32,
551-561.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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