5do7: Difference between revisions

<StructureSection load='5do7' size='340' side='right' caption='[[5do7]], [[Resolution|resolution]] 3.93&Aring;' scene=''>

<table><tr><td colspan='2'>[[5do7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DO7 FirstGlance]. <br>

</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=5do7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5do7 OCA], [http://pdbe.org/5do7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5do7 RCSB], [http://www.ebi.ac.uk/pdbsum/5do7 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ABCG5_HUMAN ABCG5_HUMAN]] Sitosterolemia. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/ABCG8_HUMAN ABCG8_HUMAN]] Sitosterolemia. Disease susceptibility may be associated with variations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  

[[http://www.uniprot.org/uniprot/ABCG5_HUMAN ABCG5_HUMAN]] Transporter that appears to play an indispensable role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile. [[http://www.uniprot.org/uniprot/ABCG8_HUMAN ABCG8_HUMAN]] Transporter that appears to play an indispensable role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile.

ATP binding cassette (ABC) transporters play critical roles in maintaining sterol balance in higher eukaryotes. The ABCG5/ABCG8 heterodimer (G5G8) mediates excretion of neutral sterols in liver and intestines. Mutations disrupting G5G8 cause sitosterolaemia, a disorder characterized by sterol accumulation and premature atherosclerosis. Here we use crystallization in lipid bilayers to determine the X-ray structure of human G5G8 in a nucleotide-free state at 3.9 A resolution, generating the first atomic model of an ABC sterol transporter. The structure reveals a new transmembrane fold that is present in a large and functionally diverse superfamily of ABC transporters. The transmembrane domains are coupled to the nucleotide-binding sites by networks of interactions that differ between the active and inactive ATPases, reflecting the catalytic asymmetry of the transporter. The G5G8 structure provides a mechanistic framework for understanding sterol transport and the disruptive effects of mutations causing sitosterolaemia.

 

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== References ==

[[Category: Borek, D M]]

[[Category: Cohen, J C]]

[[Category: Grishin, N V]]

[[Category: Hobbs, H H]]

[[Category: Kinch, L N]]

[[Category: Lee, J Y]]

[[Category: Otwinowski, Z]]

[[Category: Rosenbaum, D M]]

[[Category: Urbatsch, I L]]

[[Category: Xie, X S]]

[[Category: Transport protein]]