4YCM

Crystal structure of the calcium pump with bound marine macrolide BLS

Summary for 4YCM

• Entry DOI: 10.2210/pdb4ycm/pdb
• Related: 4YCN
• Descriptor: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, SODIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: membrane protein, p-type atpase, had fold, ca2+, ion pump, hydrolase
• Biological source: Oryctolagus cuniculus (Rabbit)
• Total number of polymer chains: 1
• Total formula weight: 111932.58

Authors

Morita, M.,Ogawa, H.,Ohno, O.,Yamori, T.,Suenaga, K.,Toyoshima, C. (deposition date: 2015-02-20, release date: 2016-01-13, Last modification date: 2020-02-05)

Primary citation

Morita, M.,Ogawa, H.,Ohno, O.,Yamori, T.,Suenaga, K.,Toyoshima, C.
Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding
Febs Lett., 589:1406-1411, 2015

PubMed Abstract: Biselyngbyasides (BLSs), macrolides from a marine cyanobacterium, are cytotoxic natural products whose target molecule is unknown. Here we report that BLSs are high affinity (Ki∼10 nM) inhibitors of Ca(2+)-pumps with a unique binding mode. The crystal structures of the Ca(2+)-pump in complex with BLSs at 3.2-3.5 Å-resolution show that BLSs bind to the pump near the cytoplasmic surface of the transmembrane region. The crystal structures and activity measurement of BLS analogs allow us to identify the structural features that confer high potency to BLSs as inhibitors of the pump.

PubMed: 25957767
DOI: 10.1016/j.febslet.2015.04.056

Experimental method

X-RAY DIFFRACTION (3.2 Å)