6y0p › Citations

X-ray free-electron laser studies reveal correlated motion during isopenicillin N synthase catalysis.

Rabe P, Kamps JJAG, Sutherlin KD, Linyard JDS, Aller P, Pham CC, Makita H, Clifton I, McDonough MA, Leissing TM, Shutin D, Lang PA, Butryn A, Brem J, Gul S, Fuller FD, Kim IS, Cheah MH, Fransson T, Bhowmick A, Young ID, O'Riordan L, Brewster AS, Pettinati I, Doyle M, Joti Y, Owada S, Tono K, Batyuk A, Hunter MS, Alonso-Mori R, Bergmann U, Owen RL, Sauter NK, Claridge TDW, Robinson CV, Yachandra VK, Yano J, Kern JF, Orville AM, Schofield CJ
Sci Adv 7 (2021)
Related entries: 6zae, 6zaf, 6zag, 6zah, 6zai, 6zaj, 6zal, 6zam, 6zan, 6zao, 6zap, 6zaq, 6zw8

Cited: 13 times
EuropePMC logo PMID: 34417180

Abstract

Isopenicillin N synthase (IPNS) catalyzes the unique reaction of l-δ-(α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) with dioxygen giving isopenicillin N (IPN), the precursor of all natural penicillins and cephalosporins. X-ray free-electron laser studies including time-resolved crystallography and emission spectroscopy reveal how reaction of IPNS:Fe(II):ACV with dioxygen to yield an Fe(III) superoxide causes differences in active site volume and unexpected conformational changes that propagate to structurally remote regions. Combined with solution studies, the results reveal the importance of protein dynamics in regulating intermediate conformations during conversion of ACV to IPN. The results have implications for catalysis by multiple IPNS-related oxygenases, including those involved in the human hypoxic response, and highlight the power of serial femtosecond crystallography to provide insight into long-range enzyme dynamics during reactions presently impossible for nonprotein catalysts.

Articles - 6y0p mentioned but not cited (1)

  1. X-ray free-electron laser studies reveal correlated motion during isopenicillin N synthase catalysis. Rabe P, Kamps JJAG, Sutherlin KD, Linyard JDS, Aller P, Pham CC, Makita H, Clifton I, McDonough MA, Leissing TM, Shutin D, Lang PA, Butryn A, Brem J, Gul S, Fuller FD, Kim IS, Cheah MH, Fransson T, Bhowmick A, Young ID, O'Riordan L, Brewster AS, Pettinati I, Doyle M, Joti Y, Owada S, Tono K, Batyuk A, Hunter MS, Alonso-Mori R, Bergmann U, Owen RL, Sauter NK, Claridge TDW, Robinson CV, Yachandra VK, Yano J, Kern JF, Orville AM, Schofield CJ. Sci Adv 7 eabh0250 (2021)


Reviews citing this publication (2)

  1. Capturing the sequence of events during the water oxidation reaction in photosynthesis using XFELs. Simon PS, Makita H, Bogacz I, Fuller F, Bhowmick A, Hussein R, Ibrahim M, Zhang M, Chatterjee R, Cheah MH, Chernev P, Doyle MD, Brewster AS, Alonso-Mori R, Sauter NK, Bergmann U, Dobbek H, Zouni A, Messinger J, Kern J, Yachandra VK, Yano J. FEBS Lett 597 30-37 (2023)
  2. Combining on-line spectroscopy with synchrotron and X-ray free electron laser crystallography. Makita H, Simon PS, Kern J, Yano J, Yachandra VK. Curr Opin Struct Biol 80 102604 (2023)

Articles citing this publication (10)

  1. Serial femtosecond crystallography. Barends TRM, Stauch B, Cherezov V, Schlichting I. Nat Rev Methods Primers 2 59 (2022)
  2. Can Second Coordination Sphere and Long-Range Interactions Modulate Hydrogen Atom Transfer in a Non-Heme Fe(II)-Dependent Histone Demethylase? Chaturvedi SS, Jaber Sathik Rifayee SB, Waheed SO, Wildey J, Warner C, Schofield CJ, Karabencheva-Christova TG, Christov CZ. JACS Au 2 2169-2186 (2022)
  3. XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase. Ohmer CJ, Dasgupta M, Patwardhan A, Bogacz I, Kaminsky C, Doyle MD, Chen PY, Keable SM, Makita H, Simon PS, Massad R, Fransson T, Chatterjee R, Bhowmick A, Paley DW, Moriarty NW, Brewster AS, Gee LB, Alonso-Mori R, Moss F, Fuller FD, Batyuk A, Sauter NK, Bergmann U, Drennan CL, Yachandra VK, Yano J, Kern JF, Ragsdale SW. J Inorg Biochem 230 111768 (2022)
  4. Going around the Kok cycle of the water oxidation reaction with femtosecond X-ray crystallography. Bhowmick A, Simon PS, Bogacz I, Hussein R, Zhang M, Makita H, Ibrahim M, Chatterjee R, Doyle MD, Cheah MH, Chernev P, Fuller FD, Fransson T, Alonso-Mori R, Brewster AS, Sauter NK, Bergmann U, Dobbek H, Zouni A, Messinger J, Kern J, Yachandra VK, Yano J. IUCrJ 10 642-655 (2023)
  5. Heterogeneity in M. tuberculosis β-lactamase inhibition by Sulbactam. Malla TN, Zielinski K, Aldama L, Bajt S, Feliz D, Hayes B, Hunter M, Kupitz C, Lisova S, Knoska J, Martin-Garcia JM, Mariani V, Pandey S, Poudyal I, Sierra RG, Tolstikova A, Yefanov O, Yoon CH, Ourmazd A, Fromme P, Schwander P, Barty A, Chapman HN, Stojkovic EA, Batyuk A, Boutet S, Phillips GN, Pollack L, Schmidt M. Nat Commun 14 5507 (2023)
  6. Integrative proteomic and physiological analyses of the molecular response to dessication-stress in Auricularia fibrillifera. Guo H, Xiong X, Wang Y, Tian H, Zhang S, Geng G. Front Plant Sci 13 995810 (2022)
  7. Micro-structured polymer fixed targets for serial crystallography at synchrotrons and XFELs. Carrillo M, Mason TJ, Karpik A, Martiel I, Kepa MW, McAuley KE, Beale JH, Padeste C. IUCrJ 10 678-693 (2023)
  8. Perspective: Structure determination of protein-ligand complexes at room temperature using X-ray diffraction approaches. Hough MA, Prischi F, Worrall JAR. Front Mol Biosci 10 1113762 (2023)
  9. Room temperature X-ray absorption spectroscopy of metalloenzymes with drop-on-demand sample delivery at XFELs. Bogacz I, Makita H, Simon PS, Zhang M, Doyle MD, Chatterjee R, Fransson T, Weninger C, Fuller F, Gee L, Sato T, Seaberg M, Alonso-Mori R, Bergmann U, Yachandra VK, Kern J, Yano J. Pure Appl Chem 95 891-897 (2023)
  10. Spectroscopic studies reveal details of substrate-induced conformational changes distant from the active site in isopenicillin N synthase. Rabe P, Walla CC, Goodyear NK, Welsh J, Southwart R, Clifton I, Linyard JDS, Tumber A, Claridge TDW, Myers WK, Schofield CJ. J Biol Chem 298 102249 (2022)


Quick links