4bpd: Difference between revisions
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==Structure determination of an integral membrane kinase== | ==Structure determination of an integral membrane kinase== | ||
<StructureSection load='4bpd' size='340' side='right' | <StructureSection load='4bpd' size='340' side='right'caption='[[4bpd]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bpd]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4bpd]] is a 6 chain structure with sequence from [https://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=4BPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BPD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=78M:(2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE'>78M</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bpd OCA], [https://pdbe.org/4bpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bpd RCSB], [https://www.ebi.ac.uk/pdbsum/4bpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bpd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KDGL_ECOLI KDGL_ECOLI] Recycling of diacylglycerol produced during the turnover of membrane phospholipid. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Diacylglycerol kinase|Diacylglycerol kinase]] | *[[Diacylglycerol kinase 3D structures|Diacylglycerol kinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Boland | [[Category: Boland C]] | ||
[[Category: Caffrey | [[Category: Caffrey M]] | ||
[[Category: Li | [[Category: Li D]] | ||
Latest revision as of 14:56, 20 December 2023
Structure determination of an integral membrane kinaseStructure determination of an integral membrane kinase
Structural highlights
FunctionKDGL_ECOLI Recycling of diacylglycerol produced during the turnover of membrane phospholipid. Publication Abstract from PubMedMembrane proteins are key elements in cell physiology and drug targeting, but getting a high-resolution structure by crystallographic means is still enormously challenging. Novel strategies are in big demand to facilitate the structure determination process that will ultimately hasten the day when sequence information alone can provide a three-dimensional model. Cell-free or in vitro expression enables rapid access to large quantities of high-quality membrane proteins suitable for an array of applications. Despite its impressive efficiency, to date only two membrane proteins produced by the in vitro approach have yielded crystal structures. Here, we have analysed synergies of cell-free expression and crystallisation in lipid mesophases for generating an X-ray structure of the integral membrane enzyme diacylglycerol kinase to 2.28-A resolution. The quality of cellular and cell-free-expressed kinase samples has been evaluated systematically by comparing (1) spectroscopic properties, (2) purity and oligomer formation, (3) lipid content and (4) functionality. DgkA is the first membrane enzyme crystallised based on cell-free expression. The study provides a basic standard for the crystallisation of cell-free-expressed membrane proteins and the methods detailed here should prove generally useful and contribute to accelerating the pace at which membrane protein structures are solved. Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination.,Boland C, Li D, Shah ST, Haberstock S, Dotsch V, Bernhard F, Caffrey M Cell Mol Life Sci. 2014 Jul 11. PMID:25012698[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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