3R4S
| Cell entry of botulinum neurotoxin type C is dependent upon interaction with two ganglioside molecules | Descriptor: | Botulinum neurotoxin type C1, N-acetyl-alpha-neuraminic acid, N-acetyl-beta-neuraminic acid | Authors: | Strotmeier, J, Gu, S, Jutzi, S, Mahrhold, S, Zhou, J, Pich, A, Bigalke, H, Rummel, A, Jin, R, Binz, T. | Deposit date: | 2011-03-17 | Release date: | 2011-06-08 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (2.15 Å) | Cite: | The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites. Mol.Microbiol., 81, 2011
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3R4U
| Cell entry of botulinum neurotoxin type C is dependent upon interaction with two ganglioside molecules | Descriptor: | Botulinum neurotoxin type C1 | Authors: | Strotmeier, J, Gu, S, Jutzi, S, Mahrhold, S, Zhou, J, Pich, A, Bigalke, H, Rummel, A, Jin, R, Binz, T. | Deposit date: | 2011-03-17 | Release date: | 2011-06-08 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites. Mol.Microbiol., 81, 2011
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2A97
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2QN0
| Structure of Botulinum neurotoxin serotype C1 light chain protease | Descriptor: | Neurotoxin, ZINC ION | Authors: | Jin, R, Sikorra, S, Stegmann, C.M, Pich, A, Binz, T, Brunger, A.T. | Deposit date: | 2007-07-17 | Release date: | 2007-09-11 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (1.75 Å) | Cite: | Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity. Biochemistry, 46, 2007
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2NM1
| Structure of BoNT/B in complex with its protein receptor | Descriptor: | Botulinum neurotoxin type B, Synaptotagmin-2 | Authors: | Jin, R, Rummel, A, Binz, T, Brunger, A.T. | Deposit date: | 2006-10-20 | Release date: | 2006-12-19 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (2.15 Å) | Cite: | Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature, 444, 2006
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1T3A
| Crystal structure of Clostridium botulinum neurotoxin type E catalytic domain | Descriptor: | CHLORIDE ION, ZINC ION, neurotoxin type E | Authors: | Agarwal, R, Eswaramoorthy, S, Kumaran, D, Binz, T, Swaminathan, S. | Deposit date: | 2004-04-26 | Release date: | 2004-06-29 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.16 Å) | Cite: | Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway Biochemistry, 43, 2004
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1T3C
| Clostridium botulinum type E catalytic domain E212Q mutant | Descriptor: | CHLORIDE ION, ZINC ION, neurotoxin type E | Authors: | Agarwal, R, Eswaramoorthy, S, Kumaran, D, Binz, T, Swaminathan, S. | Deposit date: | 2004-04-26 | Release date: | 2004-06-29 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway Biochemistry, 43, 2004
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1ZKX
| Crystal structure of Glu158Ala/Thr159Ala/Asn160Ala- a triple mutant of Clostridium botulinum neurotoxin E catalytic domain | Descriptor: | CHLORIDE ION, ZINC ION, botulinum neurotoxin type E | Authors: | Agarwal, R, Binz, T, Swaminathan, S. | Deposit date: | 2005-05-04 | Release date: | 2005-07-05 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.52 Å) | Cite: | Analysis of Active Site Residues of Botulinum Neurotoxin E by Mutational, Functional, and Structural Studies: Glu335Gln Is an Apoenzyme. Biochemistry, 44, 2005
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1YVG
| Structural analysis of the catalytic domain of tetanus neurotoxin | Descriptor: | Tetanus toxin, light chain, ZINC ION | Authors: | Rao, K.N, Kumaran, D, Binz, T, Swaminathan, S. | Deposit date: | 2005-02-15 | Release date: | 2005-03-22 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Structural analysis of the catalytic domain of tetanus neurotoxin. Toxicon, 45, 2005
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1ZKW
| Crystal structure of Arg347Ala mutant of botulinum neurotoxin E catalytic domain | Descriptor: | CHLORIDE ION, ZINC ION, botulinum neurotoxin type E | Authors: | Agarwal, R, Binz, T, Swaminathan, S. | Deposit date: | 2005-05-04 | Release date: | 2005-06-28 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.17 Å) | Cite: | Analysis of Active Site Residues of Botulinum Neurotoxin E by Mutational, Functional, and Structural Studies: Glu335Gln Is an Apoenzyme. Biochemistry, 44, 2005
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1ZL6
| Crystal structure of Tyr350Ala mutant of Clostridium botulinum neurotoxin E catalytic domain | Descriptor: | SULFATE ION, ZINC ION, botulinum neurotoxin type E | Authors: | Agarwal, R, Binz, T, Swaminathan, S. | Deposit date: | 2005-05-05 | Release date: | 2005-06-28 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | Analysis of Active Site Residues of Botulinum Neurotoxin E by Mutational, Functional, and Structural Studies: Glu335Gln Is an Apoenzyme. Biochemistry, 44, 2005
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1ZN3
| Crystal structure of Glu335Ala mutant of Clostridium botulinum neurotoxin type E | Descriptor: | CHLORIDE ION, ZINC ION, botulinum neurotoxin type E | Authors: | Agarwal, R, Binz, T, Swaminathan, S. | Deposit date: | 2005-05-11 | Release date: | 2005-07-05 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Analysis of Active Site Residues of Botulinum Neurotoxin E by Mutational, Functional, and Structural Studies: Glu335Gln Is an Apoenzyme. Biochemistry, 44, 2005
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1ZL5
| Crystal structure of Glu335Gln mutant of Clostridium botulinum neurotoxin E catalytic domain | Descriptor: | CHLORIDE ION, botulinum neurotoxin type E | Authors: | Agarwal, R, Binz, T, Swaminathan, S. | Deposit date: | 2005-05-05 | Release date: | 2005-07-05 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Analysis of Active Site Residues of Botulinum Neurotoxin E by Mutational, Functional, and Structural Studies: Glu335Gln Is an Apoenzyme. Biochemistry, 44, 2005
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2A8A
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