1YZW

The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore

1YZW の概要

• エントリーDOI: 10.2210/pdb1yzw/pdb
• 分子名称: GFP-like non-fluorescent chromoprotein, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: luminescent protein
• 由来する生物種: Heteractis crispa (leathery sea anemone)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102812.93

構造登録者

Wilmann, P.G.,Petersen, J.,Pettikiriarachchi, A.,Buckle, A.M.,Devenish, R.J.,Prescott, M.,Rossjohn, J. (登録日: 2005-02-28, 公開日: 2005-05-17, 最終更新日: 2026-03-18)

主引用文献

Wilmann, P.G.,Petersen, J.,Pettikiriarachchi, A.,Buckle, A.M.,Smith, S.C.,Olsen, S.,Perugini, M.A.,Devenish, R.J.,Prescott, M.,Rossjohn, J.
The 2.1A Crystal Structure of the Far-red Fluorescent Protein HcRed: Inherent Conformational Flexibility of the Chromophore
J.Mol.Biol., 349:223-237, 2005

PubMed Abstract: We have determined the crystal structure of HcRed, a far-red fluorescent protein isolated from Heteractis crispa, to 2.1A resolution. HcRed was observed to form a dimer, in contrast to the monomeric form of green fluorescent protein (GFP) or the tetrameric forms of the GFP-like proteins (eqFP611, Rtms5 and DsRed). Unlike the well-defined chromophore conformation observed in GFP and the GFP-like proteins, the HcRed chromophore was observed to be considerably mobile. Within the HcRed structure, the cyclic tripeptide chromophore, Glu(64)-Tyr(65)-Gly(66), was observed to adopt both a cis coplanar and a trans non-coplanar conformation. As a result of these two conformations, the hydroxyphenyl moiety of the chromophore makes distinct interactions within the interior of the beta-can. These data together with a quantum chemical model of the chromophore, suggest the cis coplanar conformation to be consistent with the fluorescent properties of HcRed, and the trans non-coplanar conformation to be consistent with non-fluorescent properties of hcCP, the chromoprotein parent of HcRed. Moreover, within the GFP-like family, it appears that where conformational freedom is permissible then flexibility in the chromophore conformation is possible.

PubMed: 15876379
DOI: 10.1016/j.jmb.2005.03.020

実験手法

X-RAY DIFFRACTION (2.1 Å)