7ra4 | pdb_00007ra4

Crystal structure of Neisseria gonorrhoeae serine acetyltransferase (CysE) in complex with serine

spinqualitylabelsall models 7ra4, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ra4 is a 3 chain structure with sequence from Neisseria gonorrhoeae FA 1090. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: SER Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5F6X0_NEIG1 Publication Abstract from PubMed Serine acetyltransferase (SAT) catalyzes the first step in the two-step pathway to synthesize L-cysteine in bacteria and plants. SAT synthesizes O-acetylserine from substrates Lserine and acetyl coenzyme A and is a key enzyme for regulating cellular cysteine levels by feedback inhibition of L-cysteine, and its involvement in the cysteine synthase complex. We have performed extensive structural and kinetic characterization of the SAT enzyme from the antibiotic-resistant pathogen Neisseria gonorrhoeae. Using X-ray crystallography, we have solved the structures of NgSAT with the non-natural ligand, L-malate (present in the crystallization screen) to 2.01 A and with the natural substrate L-serine (2.80 A) bound. Both structures are hexamers, with each monomer displaying the characteristic left-handed parallel beta-helix domain of the acyltransferase superfamily of enzymes. Each structure displays both extended and closed conformations of the C-terminal tail.  Lmalate bound in the active site results in an interesting mix of open and closed active site conformations, exhibiting a structural change mimicking the conformation of cysteine (inhibitor) bound structures from other organisms. Kinetic characterization shows competitive inhibition of L-cysteine with substrates L-serine and acetyl coenzyme A. The SAT reaction represents a key point for the regulation of cysteine biosynthesis and controlling cellular sulfur due to feedback inhibition by L-cysteine and formation of the cysteine synthase complex. Data presented here provide the structural and mechanistic basis for inhibitor design and given this enzyme is not present in humans could be explored to combat the rise of extensively antimicrobial-resistant N. gonorrhoeae. Serine acetyltransferase from Neisseria gonorrhoeae; structural and biochemical basis of inhibition.,Oldham KEA, Prentice EJ, Summers EL, Hicks JL Biochem J. 2021 Dec 10. pii: 230431. doi: 10.1042/BCJ20210564. PMID:34890451 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine acetyltransferase

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