PDB ID or protein name

1n28 » Phospholipase A2, group IIA

1n28 » Phospholipase A2, group IIA
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Topology in Secreted
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1n28 » Phospholipase A2, group IIA
Depth 3.6 ± 0.6 Å
Tilt Angle 88 ± 4°
ΔGtransfer -7.0 kcal/mol
Links to 1n28 PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution 1.5 Å
Other PDB entries representing this structure 1ayp, 1bbc, 1db4, 1db5, 1dcy, 1j1a, 1kqu, 1kvo, 1n29, 1pod, 1poe, 3u8b, 3u8d, 3u8h, 3u8i
Number of subunits 1
Experimental Verification for 1n28 » Phospholipase A2, group IIA
The orientation and a set of membrane-embedded residues (V3, L19, F23, F63, and Y111) are consistent with site-directed spin-labeling studies (V3, K10, L19, F23, and F63 - based on exposure to NiEDDA; membrane depth parameters were not evaluated) (Canaan et al. 2002). Maximal membrane binding affinity is -6.4 kcal/mol (Bezzine et al. 2002).
4 references
Bezzine, S., Bollinger, J.G., Singer, A.G., Veatch, S.L., Keller, S.L., and Gelb, M.H. 2002. On the binding preference of human groups IIA and X phospholipases A2 for membranes with anionic phospholipids. J Biol Chem. 277:48523-48534. PubMed
Canaan S, Nielsen R, Ghomashchi F, Robinson BH, Gelb MH. 2002. Unusual mode of binding of human group IIA secreted phospholipase A2 to anionic interfaces as studied by continuous wave and time domain electron paramagnetic resonance spectroscopy. J Biol Chem. 277:30984-90. PubMed
Diraviyam K, Murray D. 2006. Computational analysis of the membrane association of group IIA secreted phospholipases A2: a differential role for electrostatics. Biochemistry. 45:2584-98. PubMed
Zhou F, Schulten K. 1996. Molecular dynamics study of phospholipase A2 on a membrane surface. Proteins. 25:12-27. PubMed
Comments on 1n28 » Phospholipase A2, group IIA
Participates in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This orientation is similar to one predicted by Diraviyam and Murray (2006). However, phospholipase penetrates by ~10A deeper in the membrane according to our results and MD simulations (Zhou and Schulten, 1996): nonpolar residues are inserted in the hydrocarbon core, not in the head group region.