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PDBsum entry 1bjf
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Calcium-binding
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PDB id
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1bjf
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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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Crystal structure of recombinant bovine neurocalcin.
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Authors
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S.Vijay-Kumar,
V.D.Kumar.
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Ref.
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Nat Struct Biol, 1999,
6,
80-88.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of calcium-bound unmyristoylated bovine neurocalcin from
Escherichia coli has been determined at 2.4 A resolution. The three-dimensional
structure reveals a highly compact structure consisting of: (i) two pairs of
calcium-binding EF-hands (EF1-EF2 and EF3-EF4); (ii) a calcium ion bound at EF2,
EF3 and EF4 sites; and (iii) an EF1-hand that is disabled from calcium-binding
due to a Cys-Pro sequence in the Ca2+-binding loop. The crystal structure of
neurocalcin resembles photoreceptor recoverin in overall topology, however its
EF2- and EF4-hands differ. Recently, neurocalcin in the calcium-bound state has
been shown to stimulate mammalian rod outer segment membrane guanylate cyclase.
A possible site for cyclase activity based on the three-dimensional structure is
discussed.
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Figure 3.
Figure 3. Representation of the four EF-hands of neurocalcin
(EF1, EF2, EF3, EF4). Calcium atoms are shown in magenta,
oxygens in red, sulfur in yellow and water in red. Residues
involved in the calcium coordination are shown. a, Disabled
EF1-hand showing the location of Lys 36 and Cys 38, which
prevent the EF1-hand from binding calcium, b, Ca^2+-bound
EF2-hand, c, Ca^2+-bound EF3-hand and d, Ca^2+-bound EF4-hand.
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Figure 5.
Figure 5. Stereo view of 2|F[o] - F[c]| electron density map
contoured at 1.5  for
residues 72-78 of the EF2-hand. The corresponding residues in
bovine recoverin (73-79) are not evident due to disorder^30.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1999,
6,
80-88)
copyright 1999.
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