2HB0
 
 | | Crystal Structure of CfaE, the Adhesive Subunit of CFA/I Fimbria of Enterotoxigenic Escherichia coli | | Descriptor: | CFA/I fimbrial subunit E, DI(HYDROXYETHYL)ETHER, MALONATE ION | | Authors: | Li, Y.F, Xia, D, Poole, S, Rasulova, F, Savarino, S.J. | | Deposit date: | 2006-06-13 | | Release date: | 2007-06-26 | | Last modified: | 2011-07-13 | | Method: | X-RAY DIFFRACTION (2.3 Å) | | Cite: | A receptor-binding site as revealed by the crystal structure of CfaE, the colonization factor antigen I fimbrial adhesin of enterotoxigenic Escherichia coli.
J.Biol.Chem., 282, 2007
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2ANE
 | | Crystal structure of N-terminal domain of E.Coli Lon Protease | | Descriptor: | ATP-dependent protease La | | Authors: | Li, M, Rasulova, F, Melnikov, E.E, Rotanova, T.V, Gustchina, A, Maurizi, M.R, Wlodawer, A. | | Deposit date: | 2005-08-11 | | Release date: | 2005-11-01 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.03 Å) | | Cite: | Crystal structure of the N-terminal domain of E. coli Lon protease.
Protein Sci., 14, 2005
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1RRE
 | | Crystal structure of E.coli Lon proteolytic domain | | Descriptor: | ATP-dependent protease La, SULFATE ION | | Authors: | Botos, I, Melnikov, E.E, Cherry, S, Tropea, J.E, Khalatova, A.G, Rasulova, F, Dauter, Z, Maurizi, M.R, Rotanova, T.V, Wlodawer, A, Gustchina, A. | | Deposit date: | 2003-12-08 | | Release date: | 2004-02-03 | | Last modified: | 2021-10-27 | | Method: | X-RAY DIFFRACTION (1.75 Å) | | Cite: | The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
J.Biol.Chem., 279, 2004
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3F84
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3F83
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3F85
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1RR9
 | | Catalytic domain of E.coli Lon protease | | Descriptor: | ATP-dependent protease La, SULFATE ION | | Authors: | Botos, I, Melnikov, E.E, Cherry, S, Tropea, J.E, Khalatova, A.G, Dauter, Z, Maurizi, M.R, Rotanova, T.V, Wlodawer, A, Gustchina, A. | | Deposit date: | 2003-12-08 | | Release date: | 2003-12-23 | | Last modified: | 2021-10-27 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
J.Biol.Chem., 279, 2004
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