4nk4

Crystal structure of FabI from Candidatus Liberibacter asiaticus

spinqualitylabelsall models 4nk4, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nk4 is a 6 chain structure with sequence from Candidatus Liberibacter asiaticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Huanglongbing (HLB) is a destructive citrus disease. The leading cause of HLB is Candidatus Liberibacter asiaticus. Fatty acid biosynthesis(FAS-II)is essential for bacterial viability and has been validated as a target for the discovery of novel antibacterials agents. Enoyl-acyl carrier protein reductase (also called ENR or FabI and a product of the fabI gene) is an enzyme required in a critical step of bacterial fatty acid biosynthesis and has attracted attention as a target of novel antimicrobial agents. We determined the crystal structures of FabI from Ca. L. asiaticus in its apo-form as well as in complex with b-nicotinamide adenine dinucleotide (NAD) at 1.7 and 2.7 A resolutions, respectively, to facilitate the design and screening of small molecule inhibitors of FabI. The monomeric ClFabI is highly similar to other known FabI structures as expected, however, Unlike the typical tetramer, ClFabI exists as hexamer in crystal whereas as dimer in solution, on the other hand, the substrate binding loop which always disordered in apo form, FabI structures is ordered in apo ClFabI. Interestingly, the structure of ClFabI undergoes remarkable conformational change in the substrate-binding loop in the presence of NAD. We conclude that the signature sequence motif of FabI can be considered as Gly-(Xaa)5 -Ser-(Xaa)n-Val-Tyr-(Xaa)6 -Lys-(Xaa)n-Thr instead of Tyr-(Xaa)6 -Lys. We have further identified isoniazid as a competitive inhibitor with NADH. Crystal structures and kinetic properties of enoyl-acyl carrier protein reductase I from Candidatus Liberibacter asiaticus.,Jiang L, Gao Z, Li Y, Wang S, Dong Y Protein Sci. 2014 Jan 9. doi: 10.1002/pro.2418. PMID:24407918 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enoyl-Acyl-Carrier Protein Reductase 3D structures

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