5CJU
Isobutyryl-CoA mutase fused with bound adenosylcobalamin, GDP, Mg (holo-IcmF/GDP), and substrate n-butyryl-coenzyme A
Summary for 5CJU
| Entry DOI | 10.2210/pdb5cju/pdb |
| Related | 4XC6 4XC7 4XC8 5CJT 5CJV 5CJW |
| Descriptor | Isobutyryl-CoA mutase fused, COBALAMIN, 5'-DEOXYADENOSINE, ... (6 entities in total) |
| Functional Keywords | radical enzyme, complex, isomerase, g-protein chaperone |
| Biological source | Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) |
| Total number of polymer chains | 2 |
| Total formula weight | 251426.00 |
| Authors | Jost, M.,Drennan, C.L. (deposition date: 2015-07-15, release date: 2015-09-09, Last modification date: 2023-09-27) |
| Primary citation | Jost, M.,Born, D.A.,Cracan, V.,Banerjee, R.,Drennan, C.L. Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases. J.Biol.Chem., 290:26882-26898, 2015 Cited by PubMed Abstract: Acyl-CoA mutases are a growing class of adenosylcobalamin-dependent radical enzymes that perform challenging carbon skeleton rearrangements in primary and secondary metabolism. Members of this class of enzymes must precisely control substrate positioning to prevent oxidative interception of radical intermediates during catalysis. Our understanding of substrate specificity and catalysis in acyl-CoA mutases, however, is incomplete. Here, we present crystal structures of IcmF, a natural fusion protein variant of isobutyryl-CoA mutase, in complex with the adenosylcobalamin cofactor and four different acyl-CoA substrates. These structures demonstrate how the active site is designed to accommodate the aliphatic acyl chains of each substrate. The structures suggest that a conformational change of the 5'-deoxyadenosyl group from C2'-endo to C3'-endo could contribute to initiation of catalysis. Furthermore, detailed bioinformatic analyses guided by our structural findings identify critical determinants of acyl-CoA mutase substrate specificity and predict new acyl-CoA mutase-catalyzed reactions. These results expand our understanding of the substrate specificity and the catalytic scope of acyl-CoA mutases and could benefit engineering efforts for biotechnological applications ranging from production of biofuels and commercial products to hydrocarbon remediation. PubMed: 26318610DOI: 10.1074/jbc.M115.676890 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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