2c7l
From Proteopedia
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[[Category: phycoviolobilin]] | [[Category: phycoviolobilin]] | ||
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Revision as of 14:55, 30 October 2007
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LOW TEMPERATURE STRUCTURE OF PHYCOERYTHROCYANIN FROM MASTIGOCLADUS LAMINOSUS
Overview
Phycoerythrocyanin is the only cyanobacterial phycobiliprotein containing, phycoviolobilin as a chromophore. The phycoviolobilin chromophore is, photo-reactive; upon irradiation, the chromophore undergoes a, Z/E-isomerization involving the rotation of pyrrole-ring D. We have, determined the structure of trimeric phycoerythrocyanin at three different, experimental settings: monochromatically at 110 K and 295 K as well as, with the Laue method at 288 K. Based on their chemical structures, the, restraints for the phycoviolobilin of the alpha-subunit and for the, phycocyanobilin chromophores of the beta-subunit were newly generated, which allows a chemically meaningful refinement of both chromophores. All, three phycoerythrocyanin structures are very similar; the subunits match, within 0.5 A. ... [(full description)]
About this Structure
2C7L is a [Protein complex] structure of sequences from [Mastigocladus laminosus] with BLA and CYC as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Local protein flexibility as a prerequisite for reversible chromophore isomerization in alpha-phycoerythrocyanin., Schmidt M, Krasselt A, Reuter W, Biochim Biophys Acta. 2006 Jan;1764(1):55-62. Epub 2005 Nov 21. PMID:16377266
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