1YVG	Hydrolase	date	Feb 15, 2005
title	Structural Analysis Of The Catalytic Domain Of Tetanus Neurotoxin
authors	K.N.Rao, D.Kumaran, T.Binz, S.Swaminathan
compound		source
Molecule: Tetanus Toxin, Light Chain Chain: A Fragment: Chain L Synonym: Tentoxylysin, Light Chain Ec: 3.4.24.68 Engineered: Yes		Organism_scientific: Clostridium Tetani Organism_common: Bacteria Gene: Tetx Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_vector_type: Plasmid
symmetry	Space Group: C 2 2 2	R_factor	0.218
crystal cell	length a length b length c angle alpha angle beta angle gamma 106.610 177.280 54.550 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	2.60 Å
ligand	ZN	enzyme	Tentoxilysin;. Tetanus neurotoxin. Hydrolase E.C.3.4.24.68 BRENDA
related structures	by homologous chain: 1Z7H
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	Structural analysis of the catalytic domain of tetanus neurotoxin., Rao KN, Kumaran D, Binz T, Swaminathan S, Toxicon 2005 Jun 1;45(7):929-39. Epub 2005 Apr 13. PMID:15904688

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (71 Kb) [Save to disk] Biological Unit Coordinates (1yvg.pdb1.gz) 134 Kb CSU: Contacts of Structural Units for 1YVG Likely Quarternary Molecular Structure file(s) for 1YVG Structure Factors (152 Kb) Retrieve 1YVG in mmCIF format [Save to disk]

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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 1YVG, from MSDmotif at EBI Fold representative 1yvg from FSSP and Dali (Families of Structurally Similar Proteins)

Sequence-derived information

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

Other resources with information on 1YVG

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

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