PDB 2mqu structure summary ‹ Protein Data Bank in Europe (PDBe)

Solution NMR

Spatial structure of Hm-3, a membrane-active spider toxin affecting sodium channels

Released: 05 Nov 2014

DOI: 10.2210/pdb2mqu/pdb

Source organism: Heriaeus mellotteei

Primary publication:
Structure of membrane-active toxin from crab spider Heriaeus melloteei suggests parallel evolution of sodium channel gating modifiers in Araneomorphae and Mygalomorphae.

Berkut AA, Peigneur S, Myshkin MY, Paramonov AS, Lyukmanova EN, Arseniev AS, Grishin EV, Tytgat J, Shenkarev ZO, Vassilevski AA

J Biol Chem 290 492-504 (2015)

PMID: 25352595

Function and Biology Details

Biochemical function:

toxin activity

Biological process:

modulation of process of another organism

Cellular component:

extracellular region

Structure analysis Details

Assembly composition:

monomeric (preferred)

Assembly name:

Mu-thomitoxin-Hme1c (preferred)

PDBe Complex ID:

PDB-CPX-110949 (preferred)

Entry contents:

1 distinct polypeptide molecule

Macromolecule:

Mu-thomitoxin-Hme1c Chain: A

Molecule details ›

Chain: A
Length: 35 amino acids
Theoretical weight: 3.92 KDa
Source organism: Heriaeus mellotteei
Expression system: Escherichia coli
UniProt:

Canonical: C0HJK5 (Residues: 1-35; Coverage: 100%)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Chemical shift assignment: 72%

Refinement method: na

Expression system: Escherichia coli

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2mqu @ RCSB
2mqu @ PDBj
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2mqu @ Proteopedia

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Updated mmCIF file
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PDBML
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Chemical shifts (text)
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NMR Shifts and Constraints (NEF)
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Assembly composition XML
Assembly 1 (mmCIF; gz)
Assembly 1 (atom only; mmCIF)
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Citations

5 citation in other articles

Spider toxin inhibits gating pore currents underlying periodic paralysis.

Männikkö et al. (2018)

4 more

3 mentions without citation

Structure of membrane-active toxin from crab spider Heriaeus melloteei suggests parallel evolution of sodium channel gating modifiers in Araneomorphae and Mygalomorphae.

Berkut et al. (2015)

2 more

PDBe › 2mqu