1FV2	Toxin	date	Sep 18, 2000
title	The Hc Fragment Of Tetanus Toxin Complexed With An Analogue Of Its Ganglioside Receptor Gt1b
authors	C.Fotinou, P.Emsley, I.Black, H.Ando, H.Ishida, M.Kiso, K.A.Sinha, N.F.Fairweather, N.W.Isaacs
compound		source
Molecule: Tetanus Toxin Heavy Chain Chain: A Fragment: C-Terminal Domain Of Heavy Chain Ec: 3.4.24.68 Engineered: Yes		Organism_scientific: Clostridium Tetani Organism_common: Bacteria Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_plasmid: Pet28
symmetry	Space Group: P 1 21 1	R_factor	0.224
crystal cell	length a length b length c angle alpha angle beta angle gamma 45.849 52.172 117.353 90.00 99.55 90.00
method	X-Ray Diffraction	resolution	2.50 Å
ligand	BGC, CEQ, GAL, NGA, PO4, SIA, SLB	enzyme	Tentoxilysin;. Tetanus neurotoxin. Hydrolase E.C.3.4.24.68 BRENDA
related structures	by homologous chain: 1DFQ, 1YYN
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 crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin., Fotinou C, Emsley P, Black I, Ando H, Ishida H, Kiso M, Sinha KA, Fairweather NF, Isaacs NW, J Biol Chem 2001 Aug 24;276(34):32274-81. PMID:11418600

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (85 Kb) [Save to disk] Biological Unit Coordinates (1fv2.pdb1.gz) 81 Kb CSU: Contacts of Structural Units for 1FV2 Likely Quarternary Molecular Structure file(s) for 1FV2 Structure Factors (144 Kb) Retrieve 1FV2 in mmCIF format [Save to disk]

View 1FV2 in 3D

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1FV2, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1fv2a2, region A:1111-1315 [Jmol] [rasmolscript] [script source]     - Domain d1fv2a1, region A:865-1110 [Jmol] [rasmolscript] [script source] Fold representative 1fv2 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: [1fv2_A]

Other resources with information on 1FV2

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

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