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4ycm

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Crystal structure of the calcium pump with bound marine macrolide BLS

Structural highlights

4ycm is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AT2A1_RABIT This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).

Publication Abstract from PubMed

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 approximately 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 A-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.

Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding.,Morita M, Ogawa H, Ohno O, Yamori T, Suenaga K, Toyoshima C FEBS Lett. 2015 Jun 4;589(13):1406-11. doi: 10.1016/j.febslet.2015.04.056. Epub, 2015 May 6. PMID:25957767^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 2015 Jun 4;589(13):1406-11. doi: 10.1016/j.febslet.2015.04.056. Epub, 2015 May 6. PMID:25957767 doi:http://dx.doi.org/10.1016/j.febslet.2015.04.056

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ycm"

@@ Line 3: / Line 3: @@
 <StructureSection load='4ycm' size='340' side='right'caption='[[4ycm]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ycm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YCM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ycm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YCM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7BS:(4S,5E,8S,9E,11S,13E,15E,18R)-8-METHOXY-9,11-DIMETHYL-18-[(1Z,4E)-2-METHYLHEXA-1,4-DIEN-1-YL]-2-OXOOXACYCLOOCTADECA-5,9,13,15-TETRAEN-4-YL+3-O-METHYL-BETA-D-GLUCOPYRANOSIDE'>7BS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7BS:(4S,5E,8S,9E,11S,13E,15E,18R)-8-METHOXY-9,11-DIMETHYL-18-[(1Z,4E)-2-METHYLHEXA-1,4-DIEN-1-YL]-2-OXOOXACYCLOOCTADECA-5,9,13,15-TETRAEN-4-YL+3-O-METHYL-BETA-D-GLUCOPYRANOSIDE'>7BS</scene>, <scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ycn|4ycn]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ycm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ycm OCA], [https://pdbe.org/4ycm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ycm RCSB], [https://www.ebi.ac.uk/pdbsum/4ycm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ycm ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ycm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ycm OCA], [http://pdbe.org/4ycm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ycm RCSB], [http://www.ebi.ac.uk/pdbsum/4ycm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ycm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
+[https://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 28: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Calcium-transporting ATPase]]
 [[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Morita, M]]
+[[Category: Morita M]]
-[[Category: Ogawa, H]]
+[[Category: Ogawa H]]
-[[Category: Ohno, O]]
+[[Category: Ohno O]]
-[[Category: Suenaga, K]]
+[[Category: Suenaga K]]
-[[Category: Toyoshima, C]]
+[[Category: Toyoshima C]]
-[[Category: Yamori, T]]
+[[Category: Yamori T]]
-[[Category: Ca2+]]
-[[Category: Had fold]]
-[[Category: Hydrolase]]
-[[Category: Ion pump]]
-[[Category: Membrane protein]]
-[[Category: P-type atpase]]

4ycm

From Proteopedia

Current revision

Crystal structure of the calcium pump with bound marine macrolide BLS

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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