PDB ID or protein name

1ein » Triacylglycerol lipase, open (active) state

1ein » Triacylglycerol lipase, open (active) state
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Topology in Secreted
Topologyout side
in side
1ein » Triacylglycerol lipase, open (active) state
Depth 8.1 ± 0.8 Å
Tilt Angle 63 ± 4°
ΔGtransfer -14.5 kcal/mol
Links to 1ein PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution 3.0 Å
Other PDB entries representing this structure 1dte, 1gt6
Number of subunits 1
Experimental Verification for 1ein » Triacylglycerol lipase, open (active) state
This lipase associates with membrane by its hydrophobic surface (near the bound phosphatidyl choline) according to our calculations. That is inconsistent with two different orientations of this lipase described in ESR studies (Hedin et al. 2002, 2005). Under the experimental conditions, the protein was probably in the closed state (see 1dt5 and 1tib) and associated electrostatically only with membrane surface (no penetration) through the alternative charged spots, since the ionic strength was very low. Authors used "exposure factors" of spin-labeled residues (determined using the negatively charged spin-relaxation agent Crox), instead of the standard membrane penetration depth parameter, which is based on the contrast between two uncharged polar and nonpolar agents. The latter parameter is more reliable as follows from EPR studies of transmembrane proteins and C2 domains.
2 references
Hedin EM, Hoyrup P, Patkar SA, Vind J, Svendsen A, Fransson L, Hult K. 2002. Interfacial orientation of Thermomyces lanuginosa lipase on phospholipid vesicles investigated by electron spin resonance relaxation spectroscopy. Biochemistry. 41:14185-96. PubMed
Hedin EM, Hoyrup P, Patkar SA, Vind J, Svendsen A, Hult K. 2005. Implications of surface charge and curvature for the binding orientation of Thermomyces lanuginosus lipase on negatively charged or zwitterionic phospholipid vesicles as studied by ESR spectroscopy. Biochemistry. 44: 16658-16671. PubMed