6nrp
From Proteopedia
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==Putative short-chain dehydrogenase/reductase (SDR) from Acinetobacter baumannii== | ==Putative short-chain dehydrogenase/reductase (SDR) from Acinetobacter baumannii== | ||
| - | <StructureSection load='6nrp' size='340' side='right' caption='[[6nrp]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='6nrp' size='340' side='right'caption='[[6nrp]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6nrp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NRP OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6nrp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NRP FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabG_5, fabG_1, fabG_18, fabG_23, fabG_3, fabG_4, Aba10042_16075, B9X91_04165, CEJ63_07105, SAMEA104305229_00942, SAMEA104305242_02267, SAMEA104305268_00730, SAMEA104305271_00024, SAMEA104305315_07776, SAMEA104305320_01205, SAMEA104305325_01875, SAMEA104305337_07930 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </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=6nrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nrp OCA], [https://pdbe.org/6nrp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nrp RCSB], [https://www.ebi.ac.uk/pdbsum/6nrp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nrp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Treatments for 'superbug' infections are the focus for innovative research, as drug resistance threatens human health and medical practices globally. In particular, Acinetobacter baumannii (Ab) infections are repeatedly reported as difficult to treat due to increasing antibiotic resistance. Therefore, there is increasing need to identify novel targets in the development of different antimicrobials. Of particular interest is fatty acid synthesis, vital for the formation of phospholipids, lipopolysaccharides/lipooligosaccharides, and lipoproteins of Gram-negative envelopes. The bacterial type II fatty acid synthesis (FASII) pathway is an attractive target for the development of inhibitors and is particularly favourable due to the differences from mammalian type I fatty acid synthesis. Discrete enzymes in this pathway include two reductase enzymes: 3-oxoacyl-acyl carrier protein (ACP) reductase (FabG) and enoyl-ACP reductase (FabI). Here, we investigate annotated FabG homologs, finding a low-molecular weight 3-oxoacyl-ACP reductase, as the most likely FASII FabG candidate, and high-molecular weight 3-oxoacyl-ACP reductase (HMwFabG), showing differences in structure and coenzyme preference. To date, this is the second bacterial high-molecular weight FabG structurally characterized, following FabG4 from Mycobacterium. We show that DeltaAbHMwfabG is impaired for growth in nutrient rich media and pellicle formation. We also modelled a third 3-oxoacyl-ACP reductase, which we annotated as AbSDR. Despite containing residues for catalysis and the ACP coordinating motif, biochemical analyses showed limited activity against an acetoacetyl-CoA substrate in vitro. Inhibitors designed to target FabG proteins and thus prevent fatty acid synthesis may provide a platform for use against multidrug-resistant pathogens including A. baumannii. | ||
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| + | Insights into Acinetobacter baumannii fatty acid synthesis 3-oxoacyl-ACP reductases.,Cross EM, Adams FG, Waters JK, Aragao D, Eijkelkamp BA, Forwood JK Sci Rep. 2021 Mar 29;11(1):7050. doi: 10.1038/s41598-021-86400-1. PMID:33782435<ref>PMID:33782435</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6nrp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aciba]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Aragao, D]] | [[Category: Aragao, D]] | ||
[[Category: Cross, E M]] | [[Category: Cross, E M]] | ||
Revision as of 07:41, 25 June 2021
Putative short-chain dehydrogenase/reductase (SDR) from Acinetobacter baumannii
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