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| | ==Crystal structure of S. aureus FabI in complex with NADP and triclosan (P212121)== | | ==Crystal structure of S. aureus FabI in complex with NADP and triclosan (P212121)== |
| - | <StructureSection load='4all' size='340' side='right' caption='[[4all]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4all' size='340' side='right'caption='[[4all]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4all]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ALL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ALL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4all]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ALL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ALL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ali|4ali]], [[4alj|4alj]], [[4alk|4alk]], [[4alm|4alm]], [[4aln|4aln]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADPH,_B-specific) Enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.10 1.3.1.10] </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=4all FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4all OCA], [https://pdbe.org/4all PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4all RCSB], [https://www.ebi.ac.uk/pdbsum/4all PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4all 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=4all FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4all OCA], [http://pdbe.org/4all PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4all RCSB], [http://www.ebi.ac.uk/pdbsum/4all PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4all ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3JLH9_STAAN A0A0H3JLH9_STAAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Enoyl-Acyl-Carrier Protein Reductase|Enoyl-Acyl-Carrier Protein Reductase]] | + | *[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chang, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Kisker, C]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Schiebel, J]] | + | [[Category: Chang A]] |
| - | [[Category: Tonge, P J]] | + | [[Category: Kisker C]] |
| - | [[Category: Fatty acid biosynthesis]] | + | [[Category: Schiebel J]] |
| - | [[Category: Lipid synthesis]] | + | [[Category: Tonge PJ]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Short-chain dehydrogenase/reductase superfamily]]
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| Structural highlights
Function
A0A0H3JLH9_STAAN
Publication Abstract from PubMed
Methicillin-resistant Staphylococcus aureus (MRSA) infections constitute a serious health threat worldwide, and novel antibiotics are therefore urgently needed. The enoyl-ACP reductase (saFabI) is essential for the S. aureus fatty acid biosynthesis and, hence, serves as an attractive drug target. We have obtained a series of snapshots of this enzyme that provide a mechanistic picture of ligand and inhibitor binding, including a dimer-tetramer transition combined with extensive conformational changes. Significantly, our results reveal key differences in ligand binding and recognition compared to orthologous proteins. The remarkable observed protein flexibility rationalizes our finding that saFabI is capable of efficiently reducing branched-chain fatty acid precursors. Importantly, branched-chain fatty acids represent a major fraction of the S. aureus cell membrane and are crucial for its in vivo fitness. Our discovery thus addresses a long-standing controversy regarding the essentiality of the fatty acid biosynthesis pathway in S. aureus rationalizing saFabI as a drug target.
Staphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo Essentiality.,Schiebel J, Chang A, Lu H, Baxter MV, Tonge PJ, Kisker C Structure. 2012 May 9;20(5):802-13. PMID:22579249[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schiebel J, Chang A, Lu H, Baxter MV, Tonge PJ, Kisker C. Staphylococcus aureus FabI: Inhibition, Substrate Recognition, and Potential Implications for In Vivo Essentiality. Structure. 2012 May 9;20(5):802-13. PMID:22579249 doi:10.1016/j.str.2012.03.013
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