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Strunk, R. J., Piemonte, K. M., Petersen, N. M., Koutsioulis, D., Bouriotis, V., Perry, K., and Cole, K. E. (2014) Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis. Acta Crystallogr F Struct Biol Commun. 70, 156-9
York, N. J., Lockart, M. M., Sardar, S., Khadka, N., Shi, W., Stenkamp, R. E., Zhang, J., Kiser, P. D., and Pierce, B. S. (2021) Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center. J Biol Chem. 10.1016/j.jbc.2021.100492
York, N. J., Lockart, M. M., Sardar, S., Khadka, N., Shi, W., Stenkamp, R. E., Zhang, J., Kiser, P. D., and Pierce, B. S. (2021) Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center. J Biol Chem. 10.1016/j.jbc.2021.100492
Cramer, E. R., Starcovic, S. A., Avey, R. M., Kaya, A. I., and Robart, A. R. (2023) Structure of a 10-23 deoxyribozyme exhibiting a homodimer conformation. Commun Chem. 6, 119
Thompson, M. C., Crowley, C. S., Kopstein, J., Bobik, T. A., and Yeates, T. O. (2014) Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor. Acta Crystallogr F Struct Biol Commun. 70, 1584-90
Lee, K., Gu, S., Jin, L., Le, T. Tuc Nghi, Cheng, L. W., Strotmeier, J., Kruel, A. Magdalena, Yao, G., Perry, K., Rummel, A., and Jin, R. (2013) Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog. 9, e1003690
Klein, D. E., Choi, J. L., and Harrison, S. C. (2013) Structure of a dengue virus envelope protein late-stage fusion intermediate. J Virol. 87, 2287-93
Bale, J. B., Park, R. U., Liu, Y., Gonen, S., Gonen, T., Cascio, D., King, N. P., Yeates, T. O., and Baker, D. (2015) Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression. Protein Sci. 24, 1695-701
Schlieker, C., Weihofen, W. A., Frijns, E., Kattenhorn, L. M., Gaudet, R., and Ploegh, H. L. (2007) Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol Cell. 25, 677-87
Toms, A. V., Deshpande, A., McNally, R., Jeong, Y., Rogers, J. M., Kim, C. Un, Gruner, S. M., Ficarro, S. B., Marto, J. A., Sattler, M., Griffin, J. D., and Eck, M. J. (2013) Structure of a pseudokinase-domain switch that controls oncogenic activation of Jak kinases. Nat Struct Mol Biol. 20, 1221-3
AhYoung, A. P., Koehl, A., Vizcarra, C. L., Cascio, D., and Egea, P. F. (2016) Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen Plasmodium falciparum. Protein Sci. 25, 689-701
Benavides, B. S., Valandro, S., Cioloboc, D., Taylor, A. B., Schanze, K. S., and Kurtz, D. M. (2020) Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry. 59, 1618-1629
Keszei, A. F. A., Tang, X., McCormick, C., Zeqiraj, E., Rohde, J. R., Tyers, M., and Sicheri, F. (2014) Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol. 34, 362-73
Sharma, H., Yu, S., Kong, J., Wang, J., and Steitz, T. A. (2009) Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc Natl Acad Sci U S A. 106, 16604-9
Becker, A., Kannan, T. R., Taylor, A. B., Pakhomova, O. N., Zhang, Y., Somarajan, S. R., Galaleldeen, A., Holloway, S. P., Baseman, J. B., and P Hart, J. (2015) Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae. Proc Natl Acad Sci U S A. 112, 5165-70
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Zhao, Q., Han, Q., Kissinger, C. R., Hermann, T., and Thompson, P. A. (2008) Structure of hepatitis C virus IRES subdomain IIa. Acta Crystallogr D Biol Crystallogr. 64, 436-43
Duda, D. M., Olszewski, J. L., Schuermann, J. P., Kurinov, I., Miller, D. J., Nourse, A., Alpi, A. F., and Schulman, B. A. (2013) Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure. 21, 1030-41
Kobe, M. J., Neau, D. B., Mitchell, C. E., Bartlett, S. G., and Newcomer, M. E. (2014) The structure of human 15-lipoxygenase-2 with a substrate mimic. J Biol Chem. 289, 8562-9
Pourfarjam, Y., Ventura, J., Kurinov, I., Cho, A., Moss, J., and Kim, I. - K. (2018) Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J Biol Chem. 293, 12350-12359
Pourfarjam, Y., Ventura, J., Kurinov, I., Cho, A., Moss, J., and Kim, I. - K. (2018) Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J Biol Chem. 293, 12350-12359
Rivera-Colón, Y., Schutsky, E. K., Kita, A. Z., and Garman, S. C. (2012) The structure of human GALNS reveals the molecular basis for mucopolysaccharidosis IV A. J Mol Biol. 423, 736-51

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