4UU0

CRYSTAL STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG) IN THE PRESENCE OF 14:1 PC

Summary for 4UU0

• Entry DOI: 10.2210/pdb4uu0/pdb
• Related: 4UU1
• Descriptor: SERCA1A, OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OX Y]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER, GLYCEROL, ... (8 entities in total)
• Functional Keywords: hydrolase, ca2+-atpase, p-type atpase, cation pump, membrane protein, lipid binding, lipid binding sites, dmpc
• Biological source: ORYCTOLAGUS CUNICULUS (RABBIT)
• Total number of polymer chains: 1
• Total formula weight: 110605.05

Authors

Drachmann, N.D.,Olesen, C.,Moeller, J.V.,Guo, Z.,Nissen, P.,Bublitz, M. (deposition date: 2014-07-24, release date: 2014-10-01, Last modification date: 2024-11-06)

Primary citation

Drachmann, N.D.,Olesen, C.,Moller, J.V.,Guo, Z.,Nissen, P.,Bublitz, M.
Comparing Crystal Structures of Ca(2+) -ATPase in the Presence of Different Lipids.
FEBS J., 281:4249-, 2014

PubMed Abstract: The activity of the sarco/endoplasmic reticulum Ca(2+) -ATPase (SERCA) depends strongly on the lipid composition of the surrounding membrane. Yet, structural information on SERCA-lipid interaction is still relatively scarce, and the influence of different lipids on the enzyme is not well understood. We have analyzed SERCA crystal structures in the presence of four different phosphatidylcholine lipids of different lengths and double-bond compositions, and we find three different binding sites for lipid head groups, which are apparently independent of the acyl moiety of the lipids used. By comparison with other available SERCA structures with bound lipids, we find a total of five recurring sites, two of which are specific to certain conformational states of the enzyme, two others are state-independent, and one is a crucial site for crystal formation. Three of the binding sites overlap with or are in close vicinity to known binding sites for various SERCA-specific inhibitors and regulators, e.g. thapsigargin, sarcolipin/phospholamban and cyclopiazonic acid. Whereas the transient sites are amenable to a transient, regulatory influence of lipid molecules, the state-independent sites probably provide a flexible anchoring of the protein in the fluid bilayer.

PubMed: 25103814
DOI: 10.1111/FEBS.12957

Experimental method

X-RAY DIFFRACTION (2.5 Å)