1FV3	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, B Fragment: C-Terminal Domain Of Heavy Chain 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	0.237
crystal cell	length a length b length c angle alpha angle beta angle gamma 91.311 53.068 118.278 90.00 89.78 90.00
method	X-Ray Diffraction	resolution	2.30 Å
ligand	BGC, CEQ, GAL, NGA, PO4, SIA, SLB	enzyme
related structures	by homologous chain: 1YXW, 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, B 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] (163 Kb) [Save to disk] Biological Unit Coordinates (1fv3.pdb1.gz) 84 Kb Biological Unit Coordinates (1fv3.pdb2.gz) 78 Kb CSU: Contacts of Structural Units for 1FV3 Likely Quarternary Molecular Structure file(s) for 1FV3 Structure Factors (387 Kb) Retrieve 1FV3 in mmCIF format [Save to disk]

View 1FV3 in 3D

Proteopedia, because life has more than 2D. On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure. On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz. On AstexViewer, from MSD-EBI (viewer documentation). On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1FV3

Protein Explorer, Easier to use and more powerful than RasMol. (Win and Mac only) Noncovalent Bond Finder displays the closest contacts to ligand or interface, reports distances, walks over water bridges. Cartoon representation from PDB Cartoon Ramachandran plot from PDBSum

Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1FV3, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1fv3a2, region A:1111-1315 [Jmol] [rasmolscript] [script source]     - Domain d1fv3a1, region A:865-1110 [Jmol] [rasmolscript] [script source]     - Domain d1fv3b2, region B:1111-1315 [Jmol] [rasmolscript] [script source]     - Domain d1fv3b1, region B:865-1110 [Jmol] [rasmolscript] [script source] Fold representative 1fv3 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: [1fv3_B] [1fv3_A]

Other resources with information on 1FV3

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

Movements, Movies and Images

Images from IMB Jena Image Library of Biological Macromolecules.

You may enter another PDB ID code

Go [Back], to the [PDB Lite page], to the [OCA Search page] or to the [PDB Home page]

---

OCA© by Jaime Prilusky, 1996-2007
Bioinformatics and Biological Computing
Weizmann Institute of Science

---