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Protein Structure, Tertiary
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Definition of 'Protein Structure, Tertiary'

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

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Monday, November 23, 2009

Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex.

18 Nov 2009 Type IV pili (T4P) are bacterial virulence factors responsible for attachment to surfaces and for twitching motility, a motion that involves a succession of pilus extension and retraction cycles. In the opportunistic pathogen Pseudomonas aeruginosa, ... Read more...


A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum.

Nov 2009 The cytoplasmic protein AxDGC2 regulates cellulose synthesis in the obligate aerobe Acetobacter xylinum by controlling the cellular concentration of the cyclic dinucleotide messenger c-di-GMP. AxDGC2 contains a Per-Arnt-Sim (PAS) domain and two ... Read more...


The membrane topography of the diphtheria toxin T domain linked to the a chain reveals a transient transmembrane hairpin and potential translocation mechanisms.

Nov 2009 The diphtheria toxin T domain helps translocate the A chain of the toxin across membranes. To gain insight into translocation, the membrane topography of key residues in T domain attached to the A chain (AT protein) was compared to that in the ... Read more...

 

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Technical information about 'Protein Structure, Tertiary'

Definition: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

Descriptor UI: D017434

Alternative terms: Protein Structure, Tertiary; Tertiary Protein Structure; Protein Structures, Tertiary; Tertiary Protein Structures; Peptide Domain; Domain, Peptide; Domains, Peptide; Peptide Domains; Protein Domains; Domain, Protein; Domains, Protein; Protein Domain;

Allowable Qualifiers: drug effects; genetics; physiology; radiation effects;

Tree Number: G02.111.570.790.709.610;

History Note: 93

Technical Notes: IM general; coord NIM with specific protein (IM); PROTEIN MOTIFS see MOTIFS, AMINO ACID is available

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