Structure of a protein photocycle intermediate by millisecond time-resolved crystallography

被引：384

作者：

Genick, UK ^{[1
]}

Borgstahl, GEO ^{[1
]}

Ng, K ^{[1
]}

Ren, Z ^{[1
]}

Pradervand, C ^{[1
]}

Burke, PM ^{[1
]}

Srajer, V ^{[1
]}

Teng, TY ^{[1
]}

Schildkamp, W ^{[1
]}

McRee, DE ^{[1
]}

Moffat, K ^{[1
]}

Getzoff, ED ^{[1
]}

机构：

[1] UNIV CHICAGO, DEPT BIOCHEM & MOL BIOL, CHICAGO, IL 60637 USA

来源：

SCIENCE | 1997年 / 275卷 / 5305期

关键词：

D O I：

10.1126/science.275.5305.1471

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's phenolic oxygen. Resulting changes in shape, hydrogen bonding, and electrostatic potential at the protein surface form a likely basis for signal transduction. The structural results suggest a general framework for the interpretation of protein photocycles.

引用

页码：1471 / 1475

页数：5

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