1YYN	Hydrolase	date	Feb 25, 2005
title	A Common Binding Site For Disialyllactose And A Tri-Peptide In The C-Fragment Of Tetanus Neurotoxin
authors	J.Seetharaman, S.Eswaramoorthy, D.Kumaran, S.Swaminathan
compound		source
Molecule: Tetanus Toxin Chain: A Fragment: Residues 875-1315 Synonym: Tentoxylysin Ec: 3.4.24.68 Engineered: Yes		Organism_scientific: Clostridium Tetani Organism_common: Bacteria Expression_system: Escherichia Coli Expression_system_common: Bacteria
symmetry	Space Group: P 21 21 21	R_factor	0.255
crystal cell	length a length b length c angle alpha angle beta angle gamma 70.907 78.930 90.977 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	2.30 Å
ligand	GLA, GLC, SIA	enzyme	Tentoxilysin;. Tetanus neurotoxin. Hydrolase E.C.3.4.24.68 BRENDA
related structures	by homologous chain: 1FV2, 1FV3
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	Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin., Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S, Proteins 2005 Aug 15;61(2):288-295. PMID:16104015

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (82 Kb) [Save to disk] Biological Unit Coordinates (1yyn.pdb1.gz) 78 Kb CSU: Contacts of Structural Units for 1YYN Likely Quarternary Molecular Structure file(s) for 1YYN Retrieve 1YYN in mmCIF format [Save to disk]

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

Sequence-derived information

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

Other resources with information on 1YYN

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

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