PDB ID or protein name

1rlw » Cytosolic phospholipase A2, group IVA

1rlw » Cytosolic phospholipase A2, group IVA
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Topology in Eukaryotic plasma membrane
Topologyextracellular side
cytoplasmic side
1rlw » Cytosolic phospholipase A2, group IVA
Depth 6.4 ± 1.9 Å
Tilt Angle 57 ± 17°
ΔGtransfer -7.8 kcal/mol
Links to 1rlw PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology cytoplasmic
Resolution 2.40 Å
Other PDB entries representing this structure 1bci
Number of subunits 1
Experimental Verification for 1rlw » Cytosolic phospholipase A2, group IVA
Side-chains of residues A34, F35, G36, M38, L39, Y96, V97 and M98 penetrate into the hydrophobic core of the membrane in the calculated orientation (Y96 is in the interfacial region). Membrane depth parameters of spin-labeled cysteines were positive only in these positions (Frazier et al. 2002, Malmberg et al. 2003), cosistently with mutagenenesis/binding studies of Bittova et al. (1999). Depth parameters were close to zero for residues K32 and N95, which are located just beyond the calculated hydrophobic boundaries. Two calcium ions are located at the distances of 5.8 and 7.2 A beyond the hydrophobic boundary, i.e. 0.8 and 2.2 A, respectively, beyond the level of bulk lipid phosphates. This is consistent with positioning of these ions approximately at the level of lipid phosphates in X-ray reflectivity and EPR studies (Malkova et al. 2005, Malmberg and Falke 2005). Maximal membrane binding affinity is about -11 kcal/mol (Bittova et al. 1999, Stahelin and Cho 2001) or -6.4 kcal/mol (Nalefski et al. 2001).
7 references
Bittova L, Sumandea M, Cho W. 1999. A structure-function study of the C2 domain of cytosolic phospholipase A2. Identification of essential calcium ligands and hydrophobic membrane binding residues. J Biol Chem. 274:9665-72. PubMed
Frazier AA, Wisner MA, Malmberg NJ, Victor KG, Fanucci GE, Nalefski EA, Falke JJ, Cafiso DS. 2002. Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling. Biochemistry. 41: 6282-6292. PubMed
Malkova S, Long F, Stahelin RV, Pingali SV, Murray D, Cho W, Schlossman ML. 2005. X-ray reflectivity studies of cPLA2{alpha}-C2 domains adsorbed onto Langmuir monolayers of SOPC. Biophys J. 89: 1861-1873. PubMed
Malmberg NJ, Falke JJ. 2005. Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains. Annu Rev Biophys Biomol Struct. 34: 71-90. PubMed
Malmberg NJ, Van Buskirk DR, and Falke JJ (2003) Membrane-docking loops of the cPLA2 C2 domain: Detailed structural analysis of the protein-membrane interface via site-directed spin-labeling Biochemistry 42: 13227-13240. PubMed
Nalefski EA, Wisner MA, Chen JZ, Sprang SR, Fukuda M, Mikoshiba K, Falke JJ. 2001. C2 domains from different Ca2+ signaling pathways display functional and mechanistic diversity. Biochemistry. 40:3089-100. PubMed
Stahelin, R.V., and Cho, W. 2001. Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2. Biochemistry. 40:4672-4678. PubMed
Comments on 1rlw » Cytosolic phospholipase A2, group IVA
Orientation of this C2 domain changes little when it associates with catalytic domain (see 1cjy).