5k18

The NatB Acetyltransferase Complex Bound To bisubstrate inhibitor

spinqualitylabelsall models 5k18, resolution 2.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5k18 is a 6 chain structure with sequence from Candida albicans WO-1 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.73Å Ligands: ACE, COA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4YFL7_CANAW Publication Abstract from PubMed The NatB N-terminal acetyltransferase specifically acetylates the N-terminal group of substrate protein peptides starting with Met-Asp/Glu/Asn/Gln. How NatB recognizes and acetylates these substrates remains unknown. Here, we report crystal structures of a NatB holoenzyme from Candida albicans in the presence of its co-factor CoA and substrate peptides. The auxiliary subunit Naa25 of NatB forms a horseshoe-like deck to hold specifically its catalytic subunit Naa20. The first two amino acids Met and Asp of a substrate peptide mediate the major interactions with the active site in the Naa20 subunit. The hydrogen bonds between the substrate Asp and pocket residues of Naa20 are essential to determine the NatB substrate specificity. Moreover, a hydrogen bond between the amino group of the substrate Met and a carbonyl group in the Naa20 active site directly anchors the substrate toward acetyl-CoA. Together, these structures define a unique molecular mechanism of specific N-terminal acetylation acted by NatB. Molecular Basis of Substrate Specific Acetylation by N-Terminal Acetyltransferase NatB.,Hong H, Cai Y, Zhang S, Ding H, Wang H, Han A Structure. 2017 Apr 4;25(4):641-649.e3. doi: 10.1016/j.str.2017.03.003. PMID:28380339 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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