7d7n: Difference between revisions
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==Cryo-EM structure of human ABCB6 transporter== | ==Cryo-EM structure of human ABCB6 transporter== | ||
<StructureSection load='7d7n' size='340' side='right'caption='[[7d7n]]' scene=''> | <StructureSection load='7d7n' size='340' side='right'caption='[[7d7n]], [[Resolution|resolution]] 5.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D7N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7D7N FirstGlance]. <br> | <table><tr><td colspan='2'>[[7d7n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D7N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7D7N FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d7n OCA], [http://pdbe.org/7d7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7d7n RCSB], [http://www.ebi.ac.uk/pdbsum/7d7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7d7n ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABCB6, MTABC3, PRP, UMAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d7n OCA], [http://pdbe.org/7d7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7d7n RCSB], [http://www.ebi.ac.uk/pdbsum/7d7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7d7n ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | |||
[[http://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN]] Ocular coloboma;Dyschromatosis universalis;Colobomatous microphthalmia. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. ABCB6 mutations are involved in familial pseudohyperkalemia, a dominantly inherited condition characterized by increased serum potassium levels, measured in whole-blood specimens stored at or below room temperature. This condition is not accompanied by clinical symptoms or biological signs except for borderline abnormalities of red cell shape (PubMed:23180570).<ref>PMID:23180570</ref> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN]] Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis.<ref>PMID:10837493</ref> <ref>PMID:17006453</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human ATP-binding cassette transporter 6 of subfamily B (ABCB6) is an ABC transporter involved in the translocation toxic metals and anti-cancer drugs. Using cryo-electron microscopy, we determined the molecular structure of full-length ABCB6 in an apo state. The structure of ABCB6 unravels the architecture of a full-length ABCB transporter that harbors two N-terminal transmembrane domains which is indispensable for its ATPase activity in our in vitro assay. A slit-like substrate binding pocket of ABCB6 may accommodate the planar shape of porphyrins, and the existence of a secondary cavity near the mitochondrial intermembrane space side would further facilitate substrate release. Furthermore, the ATPase activity of ABCB6 stimulated with a variety of porphyrin substrates showed different profiles in the presence of glutathione (GSH), suggesting the action of a distinct substrate translocation mechanism depending on the use of GSH as a cofactor. | |||
Cryo-electron microscopy structure of human ABCB6 transporter.,Wang C, Cao C, Wang N, Wang X, Wang X, Zhang XC Protein Sci. 2020 Oct 2. doi: 10.1002/pro.3960. PMID:33007128<ref>PMID:33007128</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7d7n" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cao C]] | [[Category: Cao, C]] | ||
[[Category: Wang C]] | [[Category: Wang, C]] | ||
[[Category: Wang N]] | [[Category: Wang, N]] | ||
[[Category: Wang X]] | [[Category: Wang, X]] | ||
[[Category: Zhang | [[Category: Zhang, X C]] | ||
[[Category: Dimer]] | |||
[[Category: Heme]] | |||
[[Category: Membrane protein]] | |||
[[Category: Porphyrin]] | |||
[[Category: Transporter]] | |||
Revision as of 23:55, 28 October 2020
Cryo-EM structure of human ABCB6 transporterCryo-EM structure of human ABCB6 transporter
Structural highlights
Disease[ABCB6_HUMAN] Ocular coloboma;Dyschromatosis universalis;Colobomatous microphthalmia. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. ABCB6 mutations are involved in familial pseudohyperkalemia, a dominantly inherited condition characterized by increased serum potassium levels, measured in whole-blood specimens stored at or below room temperature. This condition is not accompanied by clinical symptoms or biological signs except for borderline abnormalities of red cell shape (PubMed:23180570).[1] Function[ABCB6_HUMAN] Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis.[2] [3] Publication Abstract from PubMedHuman ATP-binding cassette transporter 6 of subfamily B (ABCB6) is an ABC transporter involved in the translocation toxic metals and anti-cancer drugs. Using cryo-electron microscopy, we determined the molecular structure of full-length ABCB6 in an apo state. The structure of ABCB6 unravels the architecture of a full-length ABCB transporter that harbors two N-terminal transmembrane domains which is indispensable for its ATPase activity in our in vitro assay. A slit-like substrate binding pocket of ABCB6 may accommodate the planar shape of porphyrins, and the existence of a secondary cavity near the mitochondrial intermembrane space side would further facilitate substrate release. Furthermore, the ATPase activity of ABCB6 stimulated with a variety of porphyrin substrates showed different profiles in the presence of glutathione (GSH), suggesting the action of a distinct substrate translocation mechanism depending on the use of GSH as a cofactor. Cryo-electron microscopy structure of human ABCB6 transporter.,Wang C, Cao C, Wang N, Wang X, Wang X, Zhang XC Protein Sci. 2020 Oct 2. doi: 10.1002/pro.3960. PMID:33007128[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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