Capturing the photo‐signaling state of a photoreceptor in a steady‐state fashion by binding a transition metal complex. (30th September 2017)

• Record Type: Journal Article
• Authors: Yu, Pengyun; Song, Lei; Qin, Jun; Wang, Jianping
• Is Part Of: Protein science. Volume 26:Number 11(2017)
• Page Start: 2249
• Page End: 2256
• Publication Date: 2017-09-30
• Subjects: protein intermediate -- conformational change -- carbonyl stretching -- CORMs; Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.3284
• Languages: English
• ISSNs: 0961-8368

Abstract

Abstract: Binding a small molecule to proteins causes conformational changes, but often to a limited extent. Here, we demonstrate that the interaction of a CO‐releasing molecule (CORM3) with a photoreceptor photoactive yellow protein (PYP) drives large structural changes in the latter. The interaction of CORM3 and a mutant of PYP, Met100Ala, not only trigger the isomerization of its chromophore, p ‐coumaric acid, from its anionic trans configuration to a protonated cis configuration, but also increases the content of β‐sheet at the cost of α‐helix and random coil in the secondary structure of the protein. The CORM3 derived Met100Ala is found to highly resemble the signaling state, which is one of the key photo‐intermediates of this photoactive protein, in both protein local conformation and chromophore configuration. The organometallic reagents hold promise as protein engineering tools. This work highlights a novel approach to structurally accessing short lived intermediates of proteins in a steady‐state fashion.