Crystallographic evidence for isomeric chromophores in 3-fluorotyrosyl-green fluorescent protein

被引：19

作者：

Bae, JH ^{[1
]}

Pal, PP ^{[1
]}

Moroder, L ^{[1
]}

Huber, R ^{[1
]}

Budisa, N ^{[1
]}

机构：

[1] Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany

来源：

CHEMBIOCHEM | 2004年 / 5卷 / 05期

关键词：

chromophores; fluorotyrosine; green fluorescent protein; isomerization; selective pressure incorporation;

D O I：

10.1002/cbic.200300818

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Flipping fluorine chromophores: The unique fluorescence property of the chromophore from green fluorescent protein (GFP) of the jellyfish Aequorea victoria results from the rigid framework of its interactions with the surrounding protein matrix. The three-dimensional structure of 3-fluorotyrosine-containing "enhanced" GFP shows two conformational states of fluorine as an integral part of the chromophore in the crystalline state (see scheme). In this way, chromophore fluorination might be used as a tool to study its flipping and dynamics directly. This will certainly lead to enrichment or even a re-evaluation of the current concepts in this field.

引用

页码：720 / 722

页数：3

共 19 条

[1] Expansion of the genetic code enables design of a novel "gold'' class of green fluorescent proteins [J].

Bae, JH ;

Rubini, M ;

Jung, G ;

Wiegand, G ;

Seifert, MHJ ;

Azim, MK ;

Kim, JS ;

Zumbusch, A ;

Holak, TA ;

Moroder, L ;

Huber, R ;

Budisa, N .

JOURNAL OF MOLECULAR BIOLOGY, 2003, 328 (05) :1071-1081

[2] High-efficiency incorporation in vivo of tyrosine analogues with altered hydroxyl acidity in place of the catalytic tyrosine-14 of Δ5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni:: Effects of the modifications on isomerase kinetics [J].

Brooks, B ;

Phillips, RS ;

Benisek, WF .

BIOCHEMISTRY, 1998, 37 (27) :9738-9742

[3]

BUDISA N, 1995, EUR J BIOCHEM, V230, P788

[4]

Budisa N, 2002, ANGEW CHEM INT EDIT, V41, P4066, DOI 10.1002/1521-3773(20021104)41:21<4066::AID-ANIE4066>3.0.CO

[5]

2-6

[6] Toward the experimental codon reassignment in vivo:: protein building with an expanded amino acid repertoire [J].

Budisa, N ;

Minks, C ;

Alefelder, S ;

Wenger, W ;

Dong, FM ;

Moroder, L ;

Huber, R .

FASEB JOURNAL, 1999, 13 (01) :41-51

[7] Towards the nonstick egg: designing fluorous proteins [J].

Marsh, ENG .

CHEMISTRY & BIOLOGY, 2000, 7 (07) :R153-R157

[8] Atomic mutations at the single tryptophan residue of human recombinant annexin V: Effects on structure, stability, and activity [J].

Minks, C ;

Huber, R ;

Moroder, L ;

Budisa, N .

BIOCHEMISTRY, 1999, 38 (33) :10649-10659

[9] Towards new protein engineering: In vivo building and folding of protein shuttles for drug delivery and targeting by the selective pressure incorporation (SPI) method [J].

Minks, C ;

Alefelder, S ;

Moroder, L ;

Huber, R ;

Budisa, N .

TETRAHEDRON, 2000, 56 (48) :9431-9442

[10] Noninvasive tracing of recombinant proteins with "fluorophenylalanine-fingers" [J].

Minks, C ;

Huber, R ;

Moroder, L ;

Budisa, N .

ANALYTICAL BIOCHEMISTRY, 2000, 284 (01) :29-34

← 1 2 →