PDBsum entry 1z7h

Hydrolase

PDB id

1z7h

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Contents

			Protein chain

					426 a.a. *

			Metals

					_ZN ×2

			Waters ×328

* Residue conservation analysis

PDB id:

1z7h

Links

Name:

Hydrolase

Title:

2.3 angstrom crystal structure of tetanus neurotoxin light chain

Structure:

Tetanus toxin light chain. Chain: a. Synonym: tetanus toxin chain l. Engineered: yes. Mutation: yes

Source:

Clostridium tetani. Organism_taxid: 1513. Gene: tetx. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

2.30Å

R-factor:

0.212

R-free:

0.216

Authors:

M.A.Breidenbach,A.T.Brunger

Key ref:

M.A.Breidenbach and A.T.Brunger (2005). 2.3 A crystal structure of tetanus neurotoxin light chain. Biochemistry, 44, 7450-7457. PubMed id: 15895988 DOI: 10.1021/bi050262j

Date:

24-Mar-05

Release date:

10-May-05

PROCHECK

	Headers

	References

Protein chain

P04958 (TETX_CLOTE) - Tetanus toxin from Clostridium tetani (strain Massachusetts / E88)

Seq: Struc:

Seq: Struc:

Seq: Struc:					1315 a.a. 426 a.a.*

Key:

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.3.4.24.68 - tentoxilysin.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.

Cofactor:

Zn(2+)

DOI no: 10.1021/bi050262j	Biochemistry 44:7450-7457 (2005)
PubMed id: 15895988

2.3 A crystal structure of tetanus neurotoxin light chain.
M.A.Breidenbach, A.T.Brunger.

ABSTRACT

TeNT is the causative agent of the neuroparalytic disease tetanus. A key component of TeNT is its light chain, a Zn(2+) endopeptidase that targets SNAREs. Recent structural studies of closely related BoNT endopeptidases indicate that substrate-binding exosites remote from a conserved active site are the primary determinants of substrate specificity. Here we report the 2.3 A X-ray crystal structure of TeNT-LC, determined by combined molecular replacement and MAD phasing. As expected, the overall structure of TeNT-LC is similar to the other known CNT light chain structures, including a conserved thermolysin-like core inserted between structurally distinct amino- and carboxy-terminal regions. Differences between TeNT-LC and the other CNT light chains are mainly limited to surface features such as unique electrostatic potential profiles. An analysis of surface residue conservation reveals a pattern of relatively high variability matching the path of substrate binding around BoNT/A, possibly serving to accommodate the variations in different SNARE targets of the CNT group.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20233039

M.Montal (2010).
Botulinum neurotoxin: a marvel of protein design.

Annu Rev Biochem, 79, 591-617.

19824793

M.R.Popoff, and P.Bouvet (2009).
Clostridial toxins.

Future Microbiol, 4, 1021-1064.

18032388

A.Fischer, C.Garcia-Rodriguez, I.Geren, J.Lou, J.D.Marks, T.Nakagawa, and M.Montal (2008).
Molecular architecture of botulinum neurotoxin E revealed by single particle electron microscopy.

J Biol Chem, 283, 3997-4003.

17244603

S.Chen, J.J.Kim, and J.T.Barbieri (2007).
Mechanism of substrate recognition by botulinum neurotoxin serotype A.

J Biol Chem, 282, 9621-9627.

16765890

P.A.Meyer, P.Ye, M.Zhang, M.H.Suh, and J.Fu (2006).
Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated structural model.

Structure, 14, 973-982.

PDB code:

2b8k

16006188

M.A.Breidenbach, and A.T.Brunger (2005).
New insights into clostridial neurotoxin-SNARE interactions.

Trends Mol Med, 11, 377-381.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.