5fll

Crystal structure of the 6-carboxyhexanoate-CoA ligase (BioW) from Bacillus subtilis in complex with a Pimeloyl-adenylate

spinqualitylabelsall models 5fll, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fll is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.34Å Ligands: MG, PPV, WAQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BIOW_BACSU Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. Publication Abstract from PubMed Biotin is an essential vitamin in plants and mammals, functioning as the carbon dioxide carrier within central lipid metabolism. Bacterial pimeloyl-CoA synthetase (BioW) acts as a highly specific substrate-selection gate, ensuring the integrity of the carbon chain in biotin synthesis. BioW catalyzes the condensation of pimelic acid (C7 dicarboxylic acid) with CoASH in an ATP-dependent manner to form pimeloyl-CoA, the first dedicated biotin building block. Multiple structures of Bacillus subtilis BioW together capture all three substrates, as well as the intermediate pimeloyl-adenylate and product pyrophosphate (PPi), indicating that the enzyme uses an internal ruler to select the correct dicarboxylic acid substrate. Both the catalytic mechanism and the surprising stability of the adenylate intermediate were rationalized through site-directed mutagenesis. Building on this understanding, BioW was engineered to synthesize high-value heptanoyl (C7) and octanoyl (C8) monocarboxylic acid-CoA and C8 dicarboxylic-CoA products, highlighting the enzyme's synthetic potential. Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters.,Wang M, Moynie L, Harrison PJ, Kelly V, Piper A, Naismith JH, Campopiano DJ Nat Chem Biol. 2017 Apr 17. doi: 10.1038/nchembio.2361. PMID:28414710 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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