5a3r: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a3r]] 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=5A3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A3R FirstGlance]. <br> | <table><tr><td colspan='2'>[[5a3r]] 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=5A3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A3R FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=DL5:SPIRO(2,4,6-TRINITROBENZENE[1,2A]-O2,O3-METHYLENE-ADENOSINE+(BETA,GAMMA-METHYLENE)TRIPHOSPHATE'>DL5</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.05Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=DL5:SPIRO(2,4,6-TRINITROBENZENE[1,2A]-O2,O3-METHYLENE-ADENOSINE+(BETA,GAMMA-METHYLENE)TRIPHOSPHATE'>DL5</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5a3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3r OCA], [https://pdbe.org/5a3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a3r RCSB], [https://www.ebi.ac.uk/pdbsum/5a3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a3r ProSAT]</span></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=5a3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3r OCA], [https://pdbe.org/5a3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a3r RCSB], [https://www.ebi.ac.uk/pdbsum/5a3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a3r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 14:03, 10 January 2024
Crystal structure of the (SR) Calcium ATPase E2.BeF3- complex bound to TNP-AMPPCPCrystal structure of the (SR) Calcium ATPase E2.BeF3- complex bound to TNP-AMPPCP
Structural highlights
FunctionAT2A1_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 PubMedVanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its inhibitory mechanism have remained unresolved. We have determined the crystal structure of sarcoplasmic reticulum Ca(2+)-ATPase with bound vanadate in the absence of Ca(2+). Vanadate is bound at the catalytic site as a planar VO3(-) in complex with water and Mg(2+) in a dephosphorylation transition-state-like conformation. Validating bound VO3(-) by anomalous difference Fourier maps using long-wavelength data we also identify a hitherto undescribed Cl(-) site near the dephosphorylation site. Crystallization was facilitated by trinitrophenyl (TNP)-derivatized nucleotides that bind with the TNP moiety occupying the binding pocket that normally accommodates the adenine of ATP, rationalizing their remarkably high affinity for E2P-like conformations of the Ca(2+)-ATPase. A comparison of the configurations of bound nucleotide analogs in the E2.VO3(-) structure with that in E2.BeF3(-) (E2P ground state analog) reveals multiple binding modes to the Ca(2+)-ATPase. Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase.,Clausen JD, Bublitz M, Arnou B, Olesen C, Andersen JP, Moller JV, Nissen P Structure. 2016 Apr 5;24(4):617-23. doi: 10.1016/j.str.2016.02.018. PMID:27050689[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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