3maf

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{{Seed}}
 
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[[Image:3maf.jpg|left|200px]]
 
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==Crystal structure of StSPL (asymmetric form)==
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The line below this paragraph, containing "STRUCTURE_3maf", creates the "Structure Box" on the page.
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<StructureSection load='3maf' size='340' side='right'caption='[[3maf]], [[Resolution|resolution]] 2.97&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3maf]] 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=3MAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MAF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.971&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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>
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{{STRUCTURE_3maf| PDB=3maf | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3maf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3maf OCA], [https://pdbe.org/3maf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3maf RCSB], [https://www.ebi.ac.uk/pdbsum/3maf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3maf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q67PY4_SYMTH Q67PY4_SYMTH]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/3maf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3maf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of StSPL (asymmetric form)===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20696404}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3maf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20696404 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20696404}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3MAF is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Symbiobacterium_thermophilum Symbiobacterium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MAF OCA].
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==Reference==
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<ref group="xtra">PMID:20696404</ref><references group="xtra"/>
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[[Category: Sphinganine-1-phosphate aldolase]]
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[[Category: Symbiobacterium thermophilum]]
[[Category: Symbiobacterium thermophilum]]
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[[Category: Bourquin, F.]]
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[[Category: Bourquin F]]
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[[Category: Capitani, G.]]
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[[Category: Capitani G]]
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[[Category: Grutter, M G.]]
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[[Category: Grutter MG]]
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[[Category: Carboxy-lyase activity]]
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[[Category: Lyase]]
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[[Category: Pyridoxal phosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 18 11:44:51 2010''
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Current revision

Crystal structure of StSPL (asymmetric form)

PDB ID 3maf

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