Journal Article

PreJuSER-111980

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Crystal structure of p44, a constitutively active splice variant of visual arrestin

Granzin, J.FZJ* ; Cousin, A.FZJ* ; Weirauch, M.FZJ* ; Schlesinger, R. ; Büldt, G.FZJ* ; Batra-Safferling, R.FZJ*

2012
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.jmb.2012.01.028

Abstract: Visual arrestin specifically binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. In contrast, the p44 splice variant can terminate phototransduction by binding to nonphosphorylated light-activated rhodopsin. Here we report the crystal structure of bovine p44 at a resolution of 1.85 Å. Compared to native arrestin, the p44 structure reveals significant differences in regions crucial for receptor binding, namely flexible loop V-VI and polar core regions. Additionally, electrostatic potential is remarkably positive on the N-domain and the C-domain. The p44 structure represents an active conformation that serves as a model to explain the 'constitutive activity' found in arrestin variants.

Keyword(s): Animals (MeSH) ; Arrestin: chemistry (MeSH) ; Arrestin: genetics (MeSH) ; Arrestin: metabolism (MeSH) ; Cattle (MeSH) ; Crystallography, X-Ray: methods (MeSH) ; Genetic Variation (MeSH) ; Light Signal Transduction (MeSH) ; Models, Molecular (MeSH) ; Phosphorylation (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Tertiary: genetics (MeSH) ; RNA Splicing (MeSH) ; Rhodopsin: metabolism (MeSH) ; Static Electricity (MeSH) ; Arrestin ; Rhodopsin ; J ; arrestin (auto) ; splice variant (auto) ; p44 (auto) ; rhodopsin (auto) ; photoreceptor (auto)

Note: We are grateful to the beamline scientists at the European Synchrotron Radiation Facility (Grenoble, France) for providing assistance with the use of beamline ID14-4. We thank Oliver H. Weiergraber for comments on the manuscript, Bianca Krafft for generating the p44 clone in S. cerevisiae, and Dieter Willbold and the Russian Group ONEXIM (GB) for generous support.

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Contributing Institute(s):

1. Molekulare Biophysik (ICS-5)
2. Strukturbiochemie (ICS-6)

Research Program(s):

1. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)
2. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2012

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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