Beta-propeller

WD domain, G-beta repeat

Ribbon diagram of the C-terminal WD40 domain of Tup1 (a transcriptional co-repressor in yeast), which adopts a 7-bladed beta-propeller fold. Ribbon is colored from blue (N-terminus) to red (C-terminus). PDB 1erj [1]
Identifiers
Symbol WD40
Pfam PF00400
Pfam clan CL0186
InterPro IPR001680
PROSITE PDOC00574
SCOP 1gp2
SUPERFAMILY 1gp2
CDD cd00200

In structural biology, a beta-propeller is a type of all-β protein architecture characterized by 4 to 8 blade-shaped beta sheets arranged toroidally around a central axis. Each sheet typically has four antiparallel β-strands twisted so that the first and fourth strands are almost perpendicular to each other. The enzyme's active site is often found in the cleft formed in the center of the propeller by loops connecting the successive four-sheet motifs. Murzin proposed a geometric model to describe the structural principles of the beta propeller.[2] According to this model the seven bladed propeller was the most favoured arrangement in geometric terms.

Examples

The influenza virus protein viral neuraminidase is a six-bladed beta-propeller protein whose active form is a tetramer. It is one of two proteins present in the viral envelope and catalyzes the cleavage of sialic acid moieties from cell-membrane proteins to aid in the targeting of newly produced virions to previously uninfected cells.

The plant UV-B sensing protein UVR8 is a seven-bladed propeller which is dimeric until absorption of UV-B light, which causes dissociation.

WD40 repeats, also known as beta-transducin repeats, are short fragments found primarily in eukaryotes.[3][4] They are often assembled in 4 to 16 repeated units to form a structural domain critical for protein-protein interactions.

A beta-propeller is a critical component of LDLR (low density lipoprotein receptor) and aids in a pH based conformational change. At neutral pH the LDLR receptor is in an extended linear conformation and can bind ligands (PCSK9). At acidic pH the linear conformation changes to a hairpin structure such that ligand binding sites bind to the beta-propeller, preventing ligand binding.[5][6]

References

  1. ↑ Sprague, E. R.; Redd, M. J.; Johnson, A. D.; Wolberger, C. (2000). "Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast". The EMBO Journal. 19 (12): 3016–3027. doi:10.1093/emboj/19.12.3016. PMC 203344Freely accessible. PMID 10856245.
  2. ↑ Murzin AG (October 1992). "Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry". Proteins. 14 (2): 191–201. doi:10.1002/prot.340140206. PMID 1409568.
  3. ↑ Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (September 1994). "The ancient regulatory-protein family of WD-repeat proteins". Nature. 371 (6495): 297–300. doi:10.1038/371297a0. PMID 8090199.
  4. ↑ Smith TF, Gaitatzes C, Saxena K, Neer EJ (May 1999). "The WD repeat: a common architecture for diverse functions". Trends Biochem. Sci. 24 (5): 181–5. doi:10.1016/S0968-0004(99)01384-5. PMID 10322433.
  5. ↑ Zhang, Da-Wei (2008). "Structural requirements for PCSK9-mediated degradation of low-density lipoprotein receptor". PNAS. 105: 13045–13050. doi:10.1073/pnas.0806312105. PMC 2526098Freely accessible. PMID 18753623.
  6. ↑ Betteridge, John (2013). "PCSK9-an exciting target for reducing LDL-cholesterol levels". Nature Reviews Endocrinology. 9: 76–78. doi:10.1038/nrendo.2012.254.

External links

Further reading

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