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| | <StructureSection load='4u0o' size='340' side='right'caption='[[4u0o]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4u0o' size='340' side='right'caption='[[4u0o]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u0o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U0O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U0O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lipA2, tll0574 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</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=4u0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0o OCA], [https://pdbe.org/4u0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u0o RCSB], [https://www.ebi.ac.uk/pdbsum/4u0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u0o ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoyl_synthase Lipoyl synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.8 2.8.1.8] </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=4u0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0o OCA], [http://pdbe.org/4u0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u0o RCSB], [http://www.ebi.ac.uk/pdbsum/4u0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u0o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LIPA2_THEEB LIPA2_THEEB]] Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). | + | [https://www.uniprot.org/uniprot/LIPA2_THEVB LIPA2_THEVB] Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.[HAMAP-Rule:MF_00206] |
| | <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: Lipoyl synthase]] | + | [[Category: Thermosynechococcus vestitus BP-1]] |
| - | [[Category: Theeb]]
| + | [[Category: Dinis PC]] |
| - | [[Category: Dinis, P C]] | + | [[Category: Harmer JE]] |
| - | [[Category: Harmer, J E]] | + | [[Category: Hiscox MJ]] |
| - | [[Category: Hiscox, M J]] | + | [[Category: Roach PL]] |
| - | [[Category: Roach, P L]] | + | [[Category: Sandy J]] |
| - | [[Category: Sandy, J]] | + | |
| - | [[Category: Radical sam]]
| + | |
| - | [[Category: Sulfotransferase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
LIPA2_THEVB Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.[HAMAP-Rule:MF_00206]
Publication Abstract from PubMed
Lipoyl cofactors are essential for living organisms and are produced by the insertion of two sulfur atoms into the relatively unreactive C-H bonds of an octanoyl substrate. This reaction requires lipoyl synthase, a member of the radical SAM enzyme superfamily. Herein we present crystal structures of lipoyl synthase with two [4Fe-4S] clusters bound at opposite ends of the TIM barrel, the usual fold of the radical SAM superfamily. The cluster required for reductive SAM cleavage conserves the features of the radical SAM superfamily, but the auxiliary cluster is bound by a CX4CX5C motif unique to lipoyl synthase. The fourth ligand to the auxiliary cluster is an extremely unusual serine residue. Site directed mutants show this conserved serine ligand is essential for the sulfur insertion steps. One crystallized LipA complex contains MTA, a breakdown product of SAM, bound in the likely SAM binding site. Modelling has identified an 18 A deep channel, well-proportioned to accommodate an octanoyl substrate. These results suggest the auxiliary cluster is the likely sulfur donor, but access to a sulfide ion for the second sulfur insertion reaction requires the loss of an iron atom from the auxiliary cluster, which the serine ligand may enabled.
Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactions.,Harmer JE, Hiscox MJ, Dinis PC, Fox SJ, Iliopoulos A, Hussey JE, Sandy J, Van Beek FT, Essex JW, Roach PL Biochem J. 2014 Aug 6. PMID:25100160[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Harmer JE, Hiscox MJ, Dinis PC, Fox SJ, Iliopoulos A, Hussey JE, Sandy J, Van Beek FT, Essex JW, Roach PL. Structures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactions. Biochem J. 2014 Aug 6. PMID:25100160 doi:http://dx.doi.org/10.1042/BJ20140895
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