1D0H	Toxin	date	Sep 10, 1999
title	The Hc Fragment Of Tetanus Toxin Complexed With N-Acetyl- Galactosamine
authors	P.Emsley, C.Fotinou, I.Black, N.F.Fairweather, I.G.Charles, C.Watts, E.Hewitt, N.W.Isaacs
compound		source
Molecule: Protein (Tetanus Toxin Hc) Chain: A Fragment: C-Terminal Domain Of Heavy Chain Synonym: Tentoxylysin Engineered: Yes Mutation: Yes		Organism_scientific: Clostridium Tetani Organism_common: Bacteria Expression_system: Escherichia Coli Expression_system_vector_type: Plasmid Expression_system_plasmid: Pet16b
symmetry	Space Group: P 21 21 21	R_factor	0.204
crystal cell	length a length b length c angle alpha angle beta angle gamma 67.076 70.882 122.238 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	2.10 Å
ligand	A2G, SO4	enzyme
related structures	by homologous chain: 1DIW, 1YXW
similarity	Belongs to the peptidase m27 family.[Toxin_trans]
subunit	The precursor polypeptide is subsequently cleaved to yield subchains l and h. These remain linked by a disulfide bridge and are non-toxic after separation.
catalytic activ.	Hydrolysis of 76-gln-|-phe-77 bond in synaptobrevin 2.
Gene	CTC ; TETX (C. tetani)
function	It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. Tetanus toxin acts by inhibiting neurotransmitter release. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the 76-gln-|-phe-77 bond of synaptobrevin-2.
Gene Ontology	Chain Function Process Component A metalloendopeptidase activit... peptidase activity metallopeptidase activity zinc ion binding hydrolase activity metal ion binding proteolysis pathogenesis extracellular region
Primary reference	The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding., Emsley P, Fotinou C, Black I, Fairweather NF, Charles IG, Watts C, Hewitt E, Isaacs NW, J Biol Chem 2000 Mar 24;275(12):8889-94. PMID:10722735

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (86 Kb) [Save to disk] Biological Unit Coordinates (1d0h.pdb1.gz) 84 Kb CSU: Contacts of Structural Units for 1D0H Likely Quarternary Molecular Structure file(s) for 1D0H Structure Factors (333 Kb) Retrieve 1D0H in mmCIF format [Save to disk]

View 1D0H in 3D

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Structure-derived information

Electron Density related parameters from EDS Electron Density Server, at Upsala Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1D0H, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1d0ha2, region A:1111-1315 [Jmol] [rasmolscript] [script source]     - Domain d1d0ha1, region A:875-1110 [Jmol] [rasmolscript] [script source] Fold representative 1d0h from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1d0h_A]

Other resources with information on 1D0H

InterPro: IPR006025 , IPR012500 , IPR011591 , IPR012928 , IPR000395 PDBREPORT (protein verification by WHAT_CHECK procedures) MMDB (Entrez's Structure Database)

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