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| | <StructureSection load='3a2b' size='340' side='right'caption='[[3a2b]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3a2b' size='340' side='right'caption='[[3a2b]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"cytophaga_keratolytica"_(kitamikado_and_ito_1979)_imai_1985 "cytophaga keratolytica" (kitamikado and ito 1979) imai 1985]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A2B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobacterium_multivorum Sphingobacterium multivorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A2B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spt ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28454 "Cytophaga keratolytica" (Kitamikado and Ito 1979) Imai 1985])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Serine_C-palmitoyltransferase Serine C-palmitoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.50 2.3.1.50] </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=3a2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a2b OCA], [https://pdbe.org/3a2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a2b RCSB], [https://www.ebi.ac.uk/pdbsum/3a2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a2b ProSAT]</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=3a2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a2b OCA], [https://pdbe.org/3a2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a2b RCSB], [https://www.ebi.ac.uk/pdbsum/3a2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a2b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SPT_SPHMU SPT_SPHMU] Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine (PubMed:17557831). Exhibits a broad substrate specificity concerning the chain length and the degree of unsaturation of acyl-CoA (PubMed:17557831).<ref>PMID:17557831</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[Serine palmitoyltransferase|Serine palmitoyltransferase]] | | *[[Serine palmitoyltransferase|Serine palmitoyltransferase]] |
| | + | *[[Serine palmitoyltransferase 3D structures|Serine palmitoyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Serine C-palmitoyltransferase]] | + | [[Category: Sphingobacterium multivorum]] |
| - | [[Category: Hoseki, J]] | + | [[Category: Hoseki J]] |
| - | [[Category: Okamoto, A]] | + | [[Category: Okamoto A]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Vitamin b6-dependent enzyme fold type i]]
| + | |
| Structural highlights
Function
SPT_SPHMU Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine (PubMed:17557831). Exhibits a broad substrate specificity concerning the chain length and the degree of unsaturation of acyl-CoA (PubMed:17557831).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Serine palmitoyltransferase (SPT) is a key enzyme of sphingolipid biosynthesis and catalyses the pyridoxal 5'-phosphate (PLP)-dependent decarboxylative condensation reaction of l-serine with palmitoyl-CoA to generate 3-ketodihydrosphingosine. The crystal structure of SPT from Sphingobacterium multivorum GTC97 complexed with l-serine was determined at 2.3 A resolution. The electron density map showed the Schiff base formation between l-serine and PLP in the crystal. Because of the hydrogen bond formation with His138, the orientation of the Calpha-H bond of the PLP-l-serine aldimine was not perpendicular to the PLP-Schiff base plane. This conformation is unfavourable for the alpha-proton abstraction by Lys244 and the reaction is expected to stop at the PLP-l-serine aldimine. Structural modelling of the following intermediates indicated that His138 changes its hydrogen bond partner from the carboxyl group of l-serine to the carbonyl group of palmitoyl-CoA upon the binding of palmitoyl-CoA, making the l-serine Calpha-H bond perpendicular to the PLP-Schiff base plane. These crystal and model structures well explained the observations on bacterial SPTs that the alpha-deprotonation of l-serine occurs only in the presence of palmitoyl-CoA. This study provides the structural evidence that directly supports our proposed mechanism of the substrate synergism in the SPT reaction.
Structural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorum.,Ikushiro H, Islam MM, Okamoto A, Hoseki J, Murakawa T, Fujii S, Miyahara I, Hayashi H J Biochem. 2009 Oct;146(4):549-62. Epub 2009 Jun 29. PMID:19564159[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ikushiro H, Islam MM, Tojo H, Hayashi H. Molecular characterization of membrane-associated soluble serine palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii. J Bacteriol. 2007 Aug;189(15):5749-61. PMID:17557831 doi:10.1128/JB.00194-07
- ↑ Ikushiro H, Islam MM, Okamoto A, Hoseki J, Murakawa T, Fujii S, Miyahara I, Hayashi H. Structural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorum. J Biochem. 2009 Oct;146(4):549-62. Epub 2009 Jun 29. PMID:19564159 doi:10.1093/jb/mvp100
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