4od4
From Proteopedia
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| - | + | ==Apo structure of a UbiA homolog from Aeropyrum pernix K1== | |
| - | + | <StructureSection load='4od4' size='340' side='right' caption='[[4od4]], [[Resolution|resolution]] 3.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4od4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpe Aerpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OD4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4od5|4od5]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ubiA, APE_1570 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 AERPE])</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=4od4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4od4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4od4 RCSB], [http://www.ebi.ac.uk/pdbsum/4od4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biosynthesis of ubiquinones requires the intramembrane UbiA enzyme, an archetypal member of a superfamily of prenyltransferases that generates lipophilic aromatic compounds. Mutations in eukaryotic superfamily members have been linked to cardiovascular degeneration and Parkinson's disease. To understand how quinones are produced within membranes, we report the crystal structures of an archaeal UbiA in its apo and substrate-bound states at 3.3 and 3.6 angstrom resolution, respectively. The structures reveal nine transmembrane helices and an extramembrane cap domain that surround a large central cavity containing the active site. To facilitate the catalysis inside membranes, UbiA has an unusual active site that opens laterally to the lipid bilayer. Our studies illuminate general mechanisms for substrate recognition and catalysis in the UbiA superfamily and rationalize disease-related mutations in humans. | ||
| - | + | Structural insights into ubiquinone biosynthesis in membranes.,Cheng W, Li W Science. 2014 Feb 21;343(6173):878-81. doi: 10.1126/science.1246774. PMID:24558159<ref>PMID:24558159</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Cheng, W | + | == References == |
| - | [[Category: Li, W | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aerpe]] | ||
| + | [[Category: Cheng, W]] | ||
| + | [[Category: Li, W]] | ||
[[Category: All alpha helical]] | [[Category: All alpha helical]] | ||
[[Category: Intramembrane aromatic prenyltransferase]] | [[Category: Intramembrane aromatic prenyltransferase]] | ||
[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 09:32, 5 January 2015
Apo structure of a UbiA homolog from Aeropyrum pernix K1
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