3mwn

Structure of the Novel 14 kDa Fragment of alpha-Subunit of Phycoerythrin from the Starving Cyanobacterium Phormidium Tenue

spinqualitylabelsall models 3mwn, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mwn is a 2 chain structure with sequence from Phormidium tenue. This structure supersedes the now removed PDB entry 2g9m. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: CYC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4L2N4_9CYAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The rod-like phycobilisome (PBS) in cyanobacterium is the light-harvesting complex of phycoerythrin (PE), phycocyanin (PC) and allophycocyanin (APC). The orderly degradation of PBS was observed under starvation conditions. A 14 kDa truncated fragment of alpha-subunit of PE (F-alphaPE) was identified from the degraded product. F-alphaPE was purified to homogeneity, sequenced and crystallized. The merohedrally twinned crystals with a twinning factor of approximately 0.5 were obtained. The crystal structure of F-alphaPE was determined with molecular replacement method using detwinned data and refined to an R(cryst) factor of 23.2% (R(free)=27.6%). The structure consisted of two crystallographically independent molecules in the asymmetric unit. The two molecules were designated as molecules A and B with a buried area of 200 A(2) at the interface. The structure of F-alphaPE consists of seven alpha-helices A, B, E, F, F', G and H. The first 31N-terminal residues that fold into parallel alpha-helices X and Y in other PEs are not present in the amino acid sequence of F-alphaPE. Both molecules, A and B contain two chromophore ligands, PEB1 and PEB2 in each. These are covalently linked to the polypeptide chain through Cys82 and Cys139, respectively. The superimposition of C(alpha) tracings of molecules A and B shows an r.m.s. shift of 1.0 A indicating that the structures of two independent molecules are very similar. The degradation of phycobilisome proteins under starvation stress seems to occur to supplement the requirement of amino acids for protein synthesis and to reduce the absorption of light energy. Structure of the novel 14kDa fragment of alpha-subunit of phycoerythrin from the starving cyanobacterium Phormidium tenue.,Soni BR, Hasan MI, Parmar A, Ethayathulla AS, Kumar RP, Singh NK, Sinha M, Kaur P, Yadav S, Sharma S, Madamwar D, Singh TP J Struct Biol. 2010 Sep;171(3):247-55. Epub 2010 May 28. PMID:20546902 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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