9i20: Difference between revisions

Latest revision as of 06:33, 20 August 2025

Cryo-EM structure of human SLC35B1 with ADP

Structural highlights

9i20 is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.85Å
Ligands:	ADP, PEV
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

S35B1_HUMAN ATP:ADP antiporter that catalyzes the exchange of ATP and ADP across the endoplasmic reticulum (ER) membrane. Imports ATP from the cytosol to the ER lumen and exports ADP in the opposite direction (PubMed:30154480, PubMed:35041824). Regulates ER energy metabolism and protein biogenesis. Appears to be part of a calcium-dependent ER to cytosol low energy response axis, where calcium efflux from ER to the cytosol triggers ATP import into the ER lumen to maintain sufficient ATP supply. Provides ATP to ER chaperone HSPA5 that drives protein folding and trafficking in the ER (PubMed:30154480, PubMed:35041824). Can transport dATP, UTP or UDP in exchange for ATP, but the physiological relevance of this process remains to be established (PubMed:30154480, PubMed:35041824).^[1] ^[2] ATP:ADP antiporter.^[3] ^[4] ATP:ADP antiporter.^[5]

References

↑ Klein MC, Zimmermann K, Schorr S, Landini M, Klemens PAW, Altensell J, Jung M, Krause E, Nguyen D, Helms V, Rettig J, Fecher-Trost C, Cavalié A, Hoth M, Bogeski I, Neuhaus HE, Zimmermann R, Lang S, Haferkamp I. AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum. Nat Commun. 2018 Aug 28;9(1):3489. PMID:30154480 doi:10.1038/s41467-018-06003-9
↑ Schwarzbaum PJ, Schachter J, Bredeston LM. The broad range di affinities for ATP transport across the ER membrane. J Biol Chem. 2022 Apr;298(4):101537. PMID:35041824 doi:10.1016/j.jbc.2021.101537
↑ Klein MC, Zimmermann K, Schorr S, Landini M, Klemens PAW, Altensell J, Jung M, Krause E, Nguyen D, Helms V, Rettig J, Fecher-Trost C, Cavalié A, Hoth M, Bogeski I, Neuhaus HE, Zimmermann R, Lang S, Haferkamp I. AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum. Nat Commun. 2018 Aug 28;9(1):3489. PMID:30154480 doi:10.1038/s41467-018-06003-9
↑ Schwarzbaum PJ, Schachter J, Bredeston LM. The broad range di affinities for ATP transport across the ER membrane. J Biol Chem. 2022 Apr;298(4):101537. PMID:35041824 doi:10.1016/j.jbc.2021.101537
↑ Klein MC, Zimmermann K, Schorr S, Landini M, Klemens PAW, Altensell J, Jung M, Krause E, Nguyen D, Helms V, Rettig J, Fecher-Trost C, Cavalié A, Hoth M, Bogeski I, Neuhaus HE, Zimmermann R, Lang S, Haferkamp I. AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum. Nat Commun. 2018 Aug 28;9(1):3489. PMID:30154480 doi:10.1038/s41467-018-06003-9

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Klein MC, Zimmermann K, Schorr S, Landini M, Klemens PAW, Altensell J, Jung M, Krause E, Nguyen D, Helms V, Rettig J, Fecher-Trost C, Cavalié A, Hoth M, Bogeski I, Neuhaus HE, Zimmermann R, Lang S, Haferkamp I. AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum. Nat Commun. 2018 Aug 28;9(1):3489. PMID:30154480 doi:10.1038/s41467-018-06003-9

[2] Schwarzbaum PJ, Schachter J, Bredeston LM. The broad range di affinities for ATP transport across the ER membrane. J Biol Chem. 2022 Apr;298(4):101537. PMID:35041824 doi:10.1016/j.jbc.2021.101537

[3] Klein MC, Zimmermann K, Schorr S, Landini M, Klemens PAW, Altensell J, Jung M, Krause E, Nguyen D, Helms V, Rettig J, Fecher-Trost C, Cavalié A, Hoth M, Bogeski I, Neuhaus HE, Zimmermann R, Lang S, Haferkamp I. AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum. Nat Commun. 2018 Aug 28;9(1):3489. PMID:30154480 doi:10.1038/s41467-018-06003-9

[4] Schwarzbaum PJ, Schachter J, Bredeston LM. The broad range di affinities for ATP transport across the ER membrane. J Biol Chem. 2022 Apr;298(4):101537. PMID:35041824 doi:10.1016/j.jbc.2021.101537

[5] Klein MC, Zimmermann K, Schorr S, Landini M, Klemens PAW, Altensell J, Jung M, Krause E, Nguyen D, Helms V, Rettig J, Fecher-Trost C, Cavalié A, Hoth M, Bogeski I, Neuhaus HE, Zimmermann R, Lang S, Haferkamp I. AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum. Nat Commun. 2018 Aug 28;9(1):3489. PMID:30154480 doi:10.1038/s41467-018-06003-9

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9i20 is ON HOLD  until Paper Publication
+==Cryo-EM structure of human SLC35B1 with ADP==
+<StructureSection load='9i20' size='340' side='right'caption='[[9i20]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9i20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9I20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9I20 FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PEV:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PEV</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=9i20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9i20 OCA], [https://pdbe.org/9i20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9i20 RCSB], [https://www.ebi.ac.uk/pdbsum/9i20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9i20 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/S35B1_HUMAN S35B1_HUMAN] ATP:ADP antiporter that catalyzes the exchange of ATP and ADP across the endoplasmic reticulum (ER) membrane. Imports ATP from the cytosol to the ER lumen and exports ADP in the opposite direction (PubMed:30154480, PubMed:35041824). Regulates ER energy metabolism and protein biogenesis. Appears to be part of a calcium-dependent ER to cytosol low energy response axis, where calcium efflux from ER to the cytosol triggers ATP import into the ER lumen to maintain sufficient ATP supply. Provides ATP to ER chaperone HSPA5 that drives protein folding and trafficking in the ER (PubMed:30154480, PubMed:35041824). Can transport dATP, UTP or UDP in exchange for ATP, but the physiological relevance of this process remains to be established (PubMed:30154480, PubMed:35041824).<ref>PMID:30154480</ref> <ref>PMID:35041824</ref>   ATP:ADP antiporter.<ref>PMID:30154480</ref> <ref>PMID:35041824</ref>   ATP:ADP antiporter.<ref>PMID:30154480</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Ahn D]]
+[[Category: Drew D]]
+[[Category: Gulati A]]
+[[Category: Suades A]]

9i20: Difference between revisions

Latest revision as of 06:33, 20 August 2025

Cryo-EM structure of human SLC35B1 with ADP

Structural highlights

Function

References

Contents

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