5g3p | pdb_00005g3p

Bacillus cereus formamidase (BceAmiF) acetylated at the active site.

spinqualitylabelsall models 5g3p, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g3p is a 6 chain structure with sequence from Atcc 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, EDO, NA, PEG, PG4, PGE, PO4 NonStd Res: SCY Related: 5g3o Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [E5LR94_BACCE] Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide.[HAMAP-Rule:MF_01243] Publication Abstract from PubMed Formamidases (EC 3.5.1.49) and amidases (EC 3.5.1.4) are paralogous cysteine-dependent enzymes which catalyze the conversion of amide substrates to ammonia and the corresponding carboxylic acid. Both enzymes have been suggested as an alternative pathway for ammonia production during urea shortage. Urea was proved key in the transcriptional regulation of formamidases/amidases, connecting urea level to amide metabolism. In addition, different amidases have also been shown to be inhibited by urea, pointing to urea-regulation at the enzymatic level. Although amidases have been widely studied due to its biotechnological application in the hydrolysis of aliphatic amides, up to date, only two formamidases have been extensively characterized, belonging to Helicobacter pylori (HpyAmiF) and Bacillus cereus (BceAmiF). In this work, we report the first structure of an acyl-intermediate of BceAmiF. We also report the inhibition of BceAmiF by urea, together with mass spectrometry studies confirming the S-carbamoylation of BceAmiF after urea treatment. X-ray studies of urea-soaked BceAmiF crystals showed short- and long-range rearrangements affecting oligomerization interfaces. Since cysteine-based switches are known to occur in the regulation of different metabolic and signaling pathways, our results suggest a novel S-carbamoylation-switch for the regulation of BceAmiF. This finding could relate to previous observations of unexplained modifications in the catalytic cysteine of different nitrilase superfamily members and therefore extending this regulation mechanism to the whole nitrilase superfamily. A novel cysteine carbamoyl-switch is responsible for the inhibition of formamidase, a nitrilase superfamily member.,Martinez-Rodriguez S, Conejero-Muriel M, Gavira JA Arch Biochem Biophys. 2019 Feb 15;662:151-159. doi: 10.1016/j.abb.2018.12.008., Epub 2018 Dec 5. PMID:30528776 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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