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| | <StructureSection load='4hyq' size='340' side='right'caption='[[4hyq]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='4hyq' size='340' side='right'caption='[[4hyq]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hyq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_albidoflavus"_(rossi_doria_1891)_gasperini_1894 "actinomyces albidoflavus" (rossi doria 1891) gasperini 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HYQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albidoflavus Streptomyces albidoflavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HYQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(1) Phospholipase A(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.32 3.1.1.32] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyq OCA], [https://pdbe.org/4hyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hyq RCSB], [https://www.ebi.ac.uk/pdbsum/4hyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hyq ProSAT]</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=4hyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hyq OCA], [http://pdbe.org/4hyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hyq RCSB], [http://www.ebi.ac.uk/pdbsum/4hyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hyq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/K0J3J2_9ACTN K0J3J2_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Murayama, K]] | + | [[Category: Streptomyces albidoflavus]] |
| - | [[Category: Sugimori, D]] | + | [[Category: Murayama K]] |
| - | [[Category: Glycerophospholipid]] | + | [[Category: Sugimori D]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lipase]]
| + | |
| Structural highlights
Function
K0J3J2_9ACTN
Publication Abstract from PubMed
The metal-independent lipase from Streptomyces albidoflavus NA297 (SaPLA1) is a phospholipase A1 as it preferentially hydrolyzes the sn-1 acyl ester in glycerophospholipids, yielding a fatty acid and 2-acyl-lysophospholipid. The molecular mechanism underlying the substrate binding by SaPLA1 is currently unknown. In this study, the crystal structure of SaPLA1 was determined at 1.75A resolutions by molecular replacement. A structural similarity search indicated the highest structural similarity to an esterase from Streptomyces scabies, followed by GDSL family enzymes. The SaPLA1 active site is composed of a Ser-His dyad (Ser11 and His218), whereby stabilization of the imidazole is provided by the main-chain carbonyl oxygen of Ser216, a common variation of the catalytic triad in many serine hydrolases, where this carbonyl maintains the orientation of the active site histidine residue. The hydrophobic pocket and cleft for lipid binding are adjacent to the active site, and are approximately 13-15A deep and 14-16A long. A partial polyethylene glycol structure was found in this hydrophobic pocket.
Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297.,Murayama K, Kano K, Matsumoto Y, Sugimori D J Struct Biol. 2013 May;182(2):192-6. doi: 10.1016/j.jsb.2013.02.003. Epub 2013, Feb 13. PMID:23416196[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Murayama K, Kano K, Matsumoto Y, Sugimori D. Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297. J Struct Biol. 2013 May;182(2):192-6. doi: 10.1016/j.jsb.2013.02.003. Epub 2013, Feb 13. PMID:23416196 doi:10.1016/j.jsb.2013.02.003
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