PDB ID or protein name

1poc » Phospholipase A2

1poc » Phospholipase A2
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Topology in Secreted
Topologyout side
in side
1poc » Phospholipase A2
Depth 4.0 ± 1.6 Å
Tilt Angle 60 ± 6°
ΔGtransfer -9.5 kcal/mol
Links to 1poc PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution 2.0 Å
Other PDB entries representing this structure none
Number of subunits 1
Experimental Verification for 1poc » Phospholipase A2
Calculated orientation is similar to that determined by spin-labeling studies (Lin et al. 1998). Membrane-embedded residues in the calculated orientation: I1, I2, Y3, P4, G5, K14, I78, F82, M86, and L90. Spin-labeled residues with small exposure factors to Crox: I2, K14, and I78 (others were not tested except F82 that has a slightly higher exposure factor) (Lin et al. 1998). These residues penetrate the aliphatic core, not the interfacial region of membrane, according to the calculations (consistent with position of the crystallized lipid). Protein-membrane binding involves significant hydrophobic, rather than electrostatic component (Bollinger et al. 2004). Maximal membrane binding affinity is -8.2 kcal/mol (Bollinger et al. 2004). Carbonyl groups of bound (substrate) lipid are situated ~2A above the calculated hydrocarbon membrane boundary plane.
2 references
Bollinger, J.G., Diraviyam, K., Ghomashchi, F., Murray, D., and Gelb, M.H. 2004. Interfacial binding of bee venom secreted phospholipase A2 to membranes occurs predominantly by a nonelectrostatic mechanism. Biochemistry. 43:13293-13304. PubMed
Lin, Y., Nielsen, R., Murray, D., Hubbell, W.L., Mailer, C., Robinson, B.H., and Gelb, M.H. 1998. Docking phospholipase A2 on membranes using electrostatic potential-modulated spin relaxation magnetic resonance. Science. 279:1925-1929. PubMed