PDBsum entry 4l1e

Photosynthesis

PDB id: 4l1e

Contents

Protein chains

(+ 0 more) 162 a.a.

(+ 0 more) 172 a.a.

Ligands

CYC ×5

BLA ×13

Waters ×244

PDB id:

4l1e

Name:

Photosynthesis

Title:

Crystal structure of c-phycocyanin from leptolyngbya sp. N62dm

Structure:

Phycocyanin alpha chain. Chain: a, c, e, g, i, k. Phycocyanin beta chain. Chain: b, d, f, h, j, l

Source:

Leptolyngbya sp. N62dm. Organism_taxid: 574115. Organism_taxid: 574115

Resolution:

2.61Å R-factor: 0.241 R-free: 0.281

Authors:

N.K.Singh,I.Raj,S.Gourinath,D.Madamwar

Key ref:

N.K.Singh et al. (2014). Crystal structure and interaction of phycocyanin with β-secretase: A putative therapy for Alzheimer's disease. Cns Neurol Disord Drug Targets, 13, 691-698. PubMed id: 24576002

Date:

03-Jun-13 Release date: 21-May-14

Protein chains

A0A067XG68  (A0A067XG68_9CYAN) -  Phycocyanin alpha chain from Leptolyngbya sp. N62DM

Seq: 162 a.a.

Struc: 162 a.a.

Protein chains

A0A067XG69  (A0A067XG69_9CYAN) -  Phycocyanin beta chain from Leptolyngbya sp. N62DM

Seq: 172 a.a.

Struc: 172 a.a.

Cns Neurol Disord Drug Targets 13:691-698 (2014)

PubMed id: 24576002

Crystal structure and interaction of phycocyanin with β-secretase: A putative therapy for Alzheimer's disease.

N.K.Singh, S.S.Hasan, J.Kumar, I.Raj, A.A.Pathan, A.Parmar, S.Shakil, S.Gourinath, D.Madamwar.

ABSTRACT

Alzheimer's disease (AD) represents a neurological disorder, which is caused by enzymatic degradation of an amyloid precursor protein into short peptide fragments that undergo association to form insoluble plaques. Preliminary studies suggest that cyanobacterial extracts, especially the light-harvesting protein phycocyanin, may provide a means to control the progression of the disease. However, the molecular mechanism of disease control remains elusive. In the present study, intact hexameric phycocyanin was isolated and crystallized from the cyanobacterium Leptolyngbya sp. N62DM, and the structure was solved to a resolution of 2.6 A. Molecular docking studies show that the phycocyanin αβ- dimer interacts with the enzyme β-secretase, which catalyzes the proteolysis of the amyloid precursor protein to form plaques. The molecular docking studies suggest that the interaction between phycocyanin and β-secretase is energetically more favorable than previously reported inhibitor-β-secretase interactions. Transgenic Caenorhabditis elegans worms, with a genotype to serve as an AD-model, were significantly protected by phycocyanin. Therefore, the present study provides a novel structure-based molecular mechanism of phycocyanin-mediated therapy against AD.