6l07
From Proteopedia
(Difference between revisions)
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==Crystal structure of Escherichia coli phosphatidylserine decarboxylase (PE-bound form)== | ==Crystal structure of Escherichia coli phosphatidylserine decarboxylase (PE-bound form)== | ||
| - | <StructureSection load='6l07' size='340' side='right'caption='[[6l07]]' scene=''> | + | <StructureSection load='6l07' size='340' side='right'caption='[[6l07]], [[Resolution|resolution]] 3.60Å' 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=6L07 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L07 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6l07]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L07 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L07 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=6l07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l07 OCA], [http://pdbe.org/6l07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l07 RCSB], [http://www.ebi.ac.uk/pdbsum/6l07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l07 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9TL:2-azaniumylethyl+(2R)-2,3-bis{[(9Z)-octadec-9-enoyl]oxy}propyl+phosphate'>9TL</scene></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylserine_decarboxylase Phosphatidylserine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.65 4.1.1.65] </span></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=6l07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l07 OCA], [http://pdbe.org/6l07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l07 RCSB], [http://www.ebi.ac.uk/pdbsum/6l07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l07 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A446DLT6_ECOLX A0A446DLT6_ECOLX]] Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).[HAMAP-Rule:MF_00662][SAAS:SAAS00970414] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In both prokaryotes and eukaryotes, phosphatidylethanolamine (PE), one of the most abundant membrane phospholipids, plays important roles in various membrane functions and is synthesized through the decarboxylation of phosphatidylserine (PS) by PS decarboxylases (PSDs). However, the catalysis and substrate recognition mechanisms of PSDs remain unclear. In this study, we focused on the PSD from Escherichia coli (EcPsd) and determined the crystal structures of EcPsd in the apo form and PE-bound form at resolutions of 2.6 and 3.6 A, respectively. EcPsd forms a homodimer, and each protomer has a positively charged substrate binding pocket at the active site. Structure-based mutational analyses revealed that conserved residues in the pocket are involved in PS decarboxylation. EcPsd has an N-terminal hydrophobic helical region that is important for membrane binding, thereby achieving efficient PS recognition. These results provide a structural basis for understanding the mechanism of PE biosynthesis by PSDs. | ||
| + | |||
| + | Structural Basis for Phosphatidylethanolamine Biosynthesis by Bacterial Phosphatidylserine Decarboxylase.,Watanabe Y, Watanabe Y, Watanabe S Structure. 2020 Apr 24. pii: S0969-2126(20)30125-8. doi:, 10.1016/j.str.2020.04.006. PMID:32402247<ref>PMID:32402247</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6l07" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Ecobd]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Watanabe S]] | + | [[Category: Phosphatidylserine decarboxylase]] |
| - | [[Category: Watanabe Y]] | + | [[Category: Watanabe, S]] |
| + | [[Category: Watanabe, Y]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Phosphatidylethanolamine]] | ||
| + | [[Category: Phosphatidylserine]] | ||
Revision as of 07:14, 27 May 2020
Crystal structure of Escherichia coli phosphatidylserine decarboxylase (PE-bound form)
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