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E
Englert, M., Xia, S., Okada, C., Nakamura, A., Tanavde, V., Yao, M., Eom, S. Hyun, Konigsberg, W. H., Söll, D., and Wang, J. (2012) Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3'-terminal phosphate and 5'-OH. Proc Natl Acad Sci U S A. 109, 15235-40
Ernst, A., Avvakumov, G., Tong, J., Fan, Y., Zhao, Y., Alberts, P., Persaud, A., Walker, J. R., Neculai, A. - M., Neculai, D., Vorobyov, A., Garg, P., Beatty, L., Chan, P. - K., Juang, Y. - C., Landry, M. - C., Yeh, C., Zeqiraj, E., Karamboulas, K., Allali-Hassani, A., Vedadi, M., Tyers, M., Moffat, J., Sicheri, F., Pelletier, L., Durocher, D., Raught, B., Rotin, D., Yang, J., Moran, M. F., Dhe-Paganon, S., and Sidhu, S. S. (2013) A strategy for modulation of enzymes in the ubiquitin system. Science. 339, 590-5
Escobar-Alvarez, S., Goldgur, Y., Yang, G., Ouerfelli, O., Li, Y., and Scheinberg, D. A. (2009) Structure and activity of human mitochondrial peptide deformylase, a novel cancer target. J Mol Biol. 387, 1211-28
Evans, R. N., Blaha, G., Bailey, S., and Steitz, T. A. (2008) The structure of LepA, the ribosomal back translocase. Proc Natl Acad Sci U S A. 105, 4673-8
F
Fagan, C. E., Maehigashi, T., Dunkle, J. A., Miles, S. J., and Dunham, C. M. (2014) Structural insights into translational recoding by frameshift suppressor tRNASufJ. RNA. 20, 1944-54
Fairman, J. Wesley, Wijerathna, S. Ranjan, Ahmad, M. Faiz, Xu, H., Nakano, R., Jha, S., Prendergast, J., R Welin, M., Flodin, S., Roos, A., Nordlund, P., Li, Z., Walz, T., and Dealwis, C. Godfrey (2011) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nat Struct Mol Biol. 18, 316-22
Fan, J., and Pavletich, N. P. (2012) Structure and conformational change of a replication protein A heterotrimer bound to ssDNA. Genes Dev. 26, 2337-47
Fan, H., Hahm, J., Diggs, S., J Perry, J. P., and Blaha, G. (2015) Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli. J Biol Chem. 290, 20856-64
Fang, J., Leichter, S. M., Jiang, J., Biswal, M., Lu, J., Zhang, Z. - M., Ren, W., Zhai, J., Cui, Q., Zhong, X., and Song, J. (2021) Substrate deformation regulates DRM2-mediated DNA methylation in plants. Sci Adv. 10.1126/sciadv.abd9224
Fath, S., Mancias, J. D., Bi, X., and Goldberg, J. (2007) Structure and organization of coat proteins in the COPII cage. Cell. 129, 1325-36
Faust, T. B., Yoon, H., Nowak, R. P., Donovan, K. A., Li, Z., Cai, Q., Eleuteri, N. A., Zhang, T., Gray, N. S., and Fischer, E. S. (2020) Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15. Nat Chem Biol. 16, 7-14
Feklistov, A., and Darst, S. A. (2011) Structural basis for promoter-10 element recognition by the bacterial RNA polymerase σ subunit.. Cell. 147, 1257-69
Feld, G. K., El-Etr, S., Corzett, M. H., Hunter, M. S., Belhocine, K., Monack, D. M., Frank, M., Segelke, B. W., and Rasley, A. (2014) Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host cell invasion. J Biol Chem. 289, 30668-30679
Feliciano, P. R., and Drennan, C. L. (2019) Structural and Biochemical Investigations of the [4Fe-4S] Cluster-Containing Fumarate Hydratase from . Biochemistry. 58, 5011-5021
Feng, L., Campbell, E. B., Hsiung, Y., and MacKinnon, R. (2010) Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science. 330, 635-41
Fenwick, M. K., and Ealick, S. E. (2020) Structural basis of elongation factor 2 switching. Curr Res Struct Biol. 2, 25-34
Fenwick, M. K., Li, Y., Cresswell, P., Modis, Y., and Ealick, S. E. (2017) Structural studies of viperin, an antiviral radical SAM enzyme. Proc Natl Acad Sci U S A. 10.1073/pnas.1705402114
Fenwick, M. K., Su, D., Dong, M., Lin, H., and Ealick, S. E. (2020) Structural Basis of the Substrate Selectivity of Viperin. Biochemistry. 10.1021/acs.biochem.9b00741
Fisher, O. S., Liu, W., Zhang, R., Stiegler, A. L., Ghedia, S., Weber, J. L., and Boggon, T. J. (2015) Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2) interaction with Krev interaction trapped 1 (KRIT1) by disease-associated mutations. J Biol Chem. 290, 2842-53
Fisher, O. S., Deng, H., Liu, D., Zhang, Y., Wei, R., Deng, Y., Zhang, F., Louvi, A., Turk, B. E., Boggon, T. J., and Su, B. (2015) Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nat Commun. 6, 7937
Fisher, O. S., Zhang, R., Li, X., Murphy, J. W., Demeler, B., and Boggon, T. J. (2013) Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. FEBS Lett. 587, 272-7
Fontán, L., Qiao, Q., Hatcher, J. M., Casalena, G., Us, I., Teater, M., Durant, M., Du, G., Xia, M., Bilchuk, N., Chennamadhavuni, S., Palladino, G., Inghirami, G., Philippar, U., Wu, H., Scott, D. A., Gray, N. S., and Melnick, A. (2018) Specific covalent inhibition of MALT1 paracaspase suppresses B cell lymphoma growth. J Clin Invest. 128, 4397-4412
G Forse, J., Ram, N., D Banatao, R., Cascio, D., Sawaya, M. R., Klock, H. E., Lesley, S. A., and Yeates, T. O. (2011) Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima. Protein Sci. 20, 168-78
Fortinez, C. Marie, Bloudoff, K., Harrigan, C., Sharon, I., Strauss, M., and T Schmeing, M. (2022) Structures and function of a tailoring oxidase in complex with a nonribosomal peptide synthetase module. Nat Commun. 13, 548
Fram, B., Su, Y., Truebridge, I., Riesselman, A. J., Ingraham, J. B., Passera, A., Napier, E., Thadani, N. N., Lim, S., Roberts, K., Kaur, G., Stiffler, M. A., Marks, D. S., Bahl, C. D., Khan, A. R., Sander, C., and Gauthier, N. P. (2024) Simultaneous enhancement of multiple functional properties using evolution-informed protein design. Nat Commun. 15, 5141

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