3ze5: Difference between revisions
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==Crystal structure of the integral membrane diacylglycerol kinase - delta4== | |||
<StructureSection load='3ze5' size='340' side='right' caption='[[3ze5]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ze5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZE5 FirstGlance]. <br> | |||
==Function== | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ze3|3ze3]], [[3ze4|3ze4]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diacylglycerol_kinase Diacylglycerol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.107 2.7.1.107] </span></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=3ze5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ze5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ze5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ze5 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/KDGL_ECOLI KDGL_ECOLI]] Recycling of diacylglycerol produced during the turnover of membrane phospholipid. | [[http://www.uniprot.org/uniprot/KDGL_ECOLI KDGL_ECOLI]] Recycling of diacylglycerol produced during the turnover of membrane phospholipid. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Diacylglycerol kinase catalyses the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid for use in shuttling water-soluble components to membrane-derived oligosaccharide and lipopolysaccharide in the cell envelope of Gram-negative bacteria. For half a century, this 121-residue kinase has served as a model for investigating membrane protein enzymology, folding, assembly and stability. Here we present crystal structures for three functional forms of this unique and paradigmatic kinase, one of which is wild type. These reveal a homo-trimeric enzyme with three transmembrane helices and an amino-terminal amphiphilic helix per monomer. Bound lipid substrate and docked ATP identify the putative active site that is of the composite, shared site type. The crystal structures rationalize extensive biochemical and biophysical data on the enzyme. They are, however, at variance with a published solution NMR model in that domain swapping, a key feature of the solution form, is not observed in the crystal structures. | |||
Crystal structure of the integral membrane diacylglycerol kinase.,Li D, Lyons JA, Pye VE, Vogeley L, Aragao D, Kenyon CP, Shah ST, Doherty C, Aherne M, Caffrey M Nature. 2013 May 23;497(7450):521-4. doi: 10.1038/nature12179. Epub 2013 May 15. PMID:23676677<ref>PMID:23676677</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Diacylglycerol kinase]] | [[Category: Diacylglycerol kinase]] | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Aragao, D | [[Category: Aragao, D]] | ||
[[Category: Caffrey, M | [[Category: Caffrey, M]] | ||
[[Category: Li, D | [[Category: Li, D]] | ||
[[Category: Lyons, J A | [[Category: Lyons, J A]] | ||
[[Category: Pye, V E | [[Category: Pye, V E]] | ||
[[Category: Vogeley, L | [[Category: Vogeley, L]] | ||
[[Category: | [[Category: 8 mag]] | ||
[[Category: Clld]] | [[Category: Clld]] | ||
[[Category: In meso crystallisation]] | [[Category: In meso crystallisation]] | ||