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PDBsum entry 1jba

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Lyase PDB id
1jba
Contents
Protein chain
189 a.a. *
Metals
_CA ×3
* Residue conservation analysis

References listed in PDB file
Key reference
Title Three-Dimensional structure of guanylyl cyclase activating protein-2, A calcium-Sensitive modulator of photoreceptor guanylyl cyclases.
Authors J.B.Ames, A.M.Dizhoor, M.Ikura, K.Palczewski, L.Stryer.
Ref. J Biol Chem, 1999, 274, 19329-19337. [DOI no: 10.1074/jbc.274.27.19329]
PubMed id 10383444
Abstract
Guanylyl cyclase activating protein-2 (GCAP-2) is a Ca2+-sensitive regulator of phototransduction in retinal photoreceptor cells. GCAP-2 activates retinal guanylyl cyclases at low Ca2+ concentration (<100 nM) and inhibits them at high Ca2+ (>500 nM). The light-induced lowering of the Ca2+ level from approximately 500 nM in the dark to approximately 50 nM following illumination is known to play a key role in visual recovery and adaptation. We report here the three-dimensional structure of unmyristoylated GCAP-2 with three bound Ca2+ ions as determined by nuclear magnetic resonance spectroscopy of recombinant, isotopically labeled protein. GCAP-2 contains four EF-hand motifs arranged in a compact tandem array like that seen previously in recoverin. The root mean square deviation of the main chain atoms in the EF-hand regions is 2.2 A in comparing the Ca2+-bound structures of GCAP-2 and recoverin. EF-1, as in recoverin, does not bind calcium because it contains a disabling Cys-Pro sequence. GCAP-2 differs from recoverin in that the calcium ion binds to EF-4 in addition to EF-2 and EF-3. A prominent exposed patch of hydrophobic residues formed by EF-1 and EF-2 (Leu24, Trp27, Phe31, Phe45, Phe48, Phe49, Tyr81, Val82, Leu85, and Leu89) may serve as a target-binding site for the transmission of calcium signals to guanylyl cyclase.
Figure 5.
Fig. 5. Schematic ribbon representation (A) and space-filling model (B) of the energy-minimized average structure of unmyristoylated GCAP-2 with three Ca^2+ bound. The side chain atoms of residues at the domain interface (Ala^63, Ala^67, Ile^103, and Ile^120) are shown in A and the color scheme is as in Fig. 4. The figure was generated using Molscript (49) and Raster3d (23).
Figure 8.
Fig. 8. Space-filling representation (A) and ball-and-stick model (B) of side chain atoms of the exposed hydrophobic patch of GCAP-2. Hydrophobic, negatively charged, and positively charged residues are highlighted in yellow, red, and blue, respectively. Solvent-exposed hydrophobic residues from EF-1 and EF-2 are indicated.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (1999, 274, 19329-19337) copyright 1999.
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