General Information

Database accession: MF4130001

Name: Tetrabrachion tetramerization region

PDB ID: 1fe6 PDB

Experimental method: X-ray (1.80 Å)

Assembly: homotetramer

Source organism: Staphylothermus marinus

Primer publication of the structure:

Stetefeld J, Jenny M, Schulthess T, Landwehr R, Engel J, Kammerer RA
Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer.

(2000) Nat. Struct. Biol. 7: 772-6

PMID: 10966648 PubMed

Abstract:

The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 A resolution. As proposed on the basis of the presence of 11-residue repeats, the polypeptide chain fragment forms a parallel right-handed coiled coil structure. Complementary hydrophobic interactions and complex networks of surface salt bridges result in an extremely thermostable tetrameric structure with remarkable properties. In marked contrast to left-handed coiled coil tetramers, the right-handed coiled coil reveals large hydrophobic cavities that are filled with water molecules. As a consequence, the packing of the hydrophobic core differs markedly from that of a right-handed parallel coiled coil tetramer that was designed on the basis of left-handed coiled coil structures.


Function and Biology Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.

Molecular function: not assigned

Biological process: not assigned

Cellular component:

integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. GeneOntology

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 4 distinct polypeptide molecules

Chains: A, B, C, D

Notes: No modifications of the original PDB file. Chain identifiers are identical with the PDB's identifiers.

Number of unique protein segments: 1


Chain A

Name: Tetrabrachion (Precursor)

Source organism: Staphylothermus marinus

Length: 52 residues

Sequence:Sequence according to PDB SEQRESGSIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASG

UniProtKB AC: Q54436 (positions: 1236-1287) UniProt Coverage: 3.4%

UniRef90 AC: UniRef90_Q54436 (positions: 1237-1286) UniRef90

Chain B

Name: Tetrabrachion (Precursor)

Source organism: Staphylothermus marinus

Length: 52 residues

Sequence:Sequence according to PDB SEQRESGSIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASG

UniProtKB AC: Q54436 (positions: 1236-1287) UniProt Coverage: 3.4%

UniRef90 AC: UniRef90_Q54436 (positions: 1237-1286) UniRef90

Chain C

Name: Tetrabrachion (Precursor)

Source organism: Staphylothermus marinus

Length: 52 residues

Sequence:Sequence according to PDB SEQRESGSIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASG

UniProtKB AC: Q54436 (positions: 1236-1287) UniProt Coverage: 3.4%

UniRef90 AC: UniRef90_Q54436 (positions: 1237-1286) UniRef90

Chain D

Name: Tetrabrachion (Precursor)

Source organism: Staphylothermus marinus

Length: 52 residues

Sequence:Sequence according to PDB SEQRESGSIINETADDIVYRLTVIIDDRYESLKNLITLRADRLEMIINDNVSTILASG

UniProtKB AC: Q54436 (positions: 1236-1287) UniProt Coverage: 3.4%

UniRef90 AC: UniRef90_Q54436 (positions: 1237-1286) UniRef90

Evidence Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding.

Complex evidence:

The subunits in the structure are bound via coiled coil interactions (PMID: 10966648). Coiled coils are highly versatile folding units (PMID: 11166216), where the formation of the structure and the interaction between subunits is almost ubiquitously linked. This cooperative nature of binding and folding that results in a two-step process has been demonstrated for coiled coils with varying oligomeric state from dimers (PMID: 9811815) and trimers (PMID: 10933510) up to heptamers (PMID: 17030805). While the interaction and folding are linked, in certain cases there can be significant residual structure before association (PMID: 8401212). However, these residual structural elements usually encompass 1-2 turns of helices that serve as a 'nucleation site' driving interaction and helix formation (zipping up) (PMID: 17438295), thus even in these cases monomeric coiled coil subunits cannot be considered to have a stable structure.

Related Structure(s) Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap).

There are 2 related structures in the Protein Data Bank:





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