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| | ==Crystal Structure of Citrate Synthase SbnG== | | ==Crystal Structure of Citrate Synthase SbnG== |
| - | <StructureSection load='4tv5' size='340' side='right' caption='[[4tv5]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='4tv5' size='340' side='right'caption='[[4tv5]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tv5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staae Staae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TV5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tv5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_str._Newman Staphylococcus aureus subsp. aureus str. Newman]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TV5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tv6|4tv6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sbnG, NWMN_0066 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=426430 STAAE])</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=4tv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tv5 OCA], [https://pdbe.org/4tv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tv5 RCSB], [https://www.ebi.ac.uk/pdbsum/4tv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tv5 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=4tv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tv5 OCA], [http://pdbe.org/4tv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tv5 RCSB], [http://www.ebi.ac.uk/pdbsum/4tv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tv5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3K9Z0_STAAE A0A0H3K9Z0_STAAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Staae]] | + | [[Category: Large Structures]] |
| - | [[Category: Grigg, J C]] | + | [[Category: Staphylococcus aureus subsp. aureus str. Newman]] |
| - | [[Category: Kobylarz, M J]]
| + | [[Category: Grigg JC]] |
| - | [[Category: Murphy, M E.P]]
| + | [[Category: Kobylarz MJ]] |
| - | [[Category: Citrate synthase]] | + | [[Category: Murphy MEP]] |
| - | [[Category: Iron]] | + | |
| - | [[Category: Lyase]] | + | |
| - | [[Category: Siderophore biosynthesis]]
| + | |
| Structural highlights
Function
A0A0H3K9Z0_STAAE
Publication Abstract from PubMed
In response to iron deprivation, Staphylococcus aureus produces staphyloferrin B, a citrate-containing siderophore that delivers iron back to the cell. This bacterium also possesses a second citrate synthase, SbnG, that is necessary for supplying citrate to the staphyloferrin B biosynthetic pathway. We present the structure of SbnG bound to the inhibitor calcium and an active site variant in complex with oxaloacetate. The overall fold of SbnG is structurally distinct from TCA cycle citrate synthases, yet similar to metal-dependent class II aldolases. Phylogenetic analyses revealed that SbnG forms a separate clade with homologs from other siderophore biosynthetic gene clusters and is representative of a metal-independent subgroup in the phosphoenolpyruvate/pyruvate domain superfamily. A structural superposition of the SbnG active site to TCA cycle citrate synthases and site-directed mutagenesis suggests a case for convergent evolution towards a conserved catalytic mechanism for citrate production.
SbnG, a Citrate Synthase in Staphylococcus aureus: a New Fold on an Old Enzyme.,Kobylarz MJ, Grigg JC, Sheldon JR, Heinrichs DE, Murphy ME J Biol Chem. 2014 Oct 21. pii: jbc.M114.603175. PMID:25336653[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kobylarz MJ, Grigg JC, Sheldon JR, Heinrichs DE, Murphy ME. SbnG, a Citrate Synthase in Staphylococcus aureus: a New Fold on an Old Enzyme. J Biol Chem. 2014 Oct 21. pii: jbc.M114.603175. PMID:25336653 doi:http://dx.doi.org/10.1074/jbc.M114.603175
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