3mad
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal structure of StSPL (symmetric form)== | ==Crystal structure of StSPL (symmetric form)== | ||
| - | <StructureSection load='3mad' size='340' side='right' caption='[[3mad]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3mad' size='340' side='right'caption='[[3mad]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3mad]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3mad]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Symbiobacterium_thermophilum Symbiobacterium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MAD 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]] 2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3mad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mad OCA], [https://pdbe.org/3mad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mad RCSB], [https://www.ebi.ac.uk/pdbsum/3mad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mad ProSAT]</span></td></tr> | |
| - | + | ||
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q67PY4_SYMTH Q67PY4_SYMTH] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 21: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mad ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mad ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Sphingosine-1-phosphate lyase (SPL), a key enzyme of sphingolipid metabolism, catalyzes the irreversible degradation of sphingoid base phosphates. Its main substrate sphingosine-1-phosphate (S1P) acts both extracellularly, by binding G protein-coupled receptors of the lysophospholipid receptor family, and inside the cell, as a second messenger. There, S1P takes part in regulating various cellular processes and its levels are tightly regulated. SPL is a pivotal enzyme regulating S1P intracellular concentrations and a promising drug target for the design of immunosuppressants. We structurally and functionally characterized yeast SPL (Dpl1p) and its first prokaryotic homolog, from Symbiobacterium thermophilum. The Dpl1p structure served as a basis for a very reliable model of Homo sapiens SPL. The above results, together with in vitro and in vivo studies of SPL mutants, reveal which residues are involved in activity and substrate binding and pave the way to studies aimed at controlling the activity of this pivotal enzyme. | ||
| - | |||
| - | Structure and function of sphingosine-1-phosphate lyase, a key enzyme of sphingolipid metabolism.,Bourquin F, Riezman H, Capitani G, Grutter MG Structure. 2010 Aug 11;18(8):1054-65. PMID:20696404<ref>PMID:20696404</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3mad" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Symbiobacterium thermophilum]] |
| - | [[Category: Bourquin | + | [[Category: Bourquin F]] |
| - | [[Category: Capitani | + | [[Category: Capitani G]] |
| - | [[Category: Grutter | + | [[Category: Grutter MG]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of StSPL (symmetric form)
| |||||||||||
