Raman spectroscopy adds complementary detail to the high-resolution x-ray crystal structure of photosynthetic PsbP from Spinacia oleracea

Autor: Rüdiger Ettrich, Jaroslava Kohoutova, David Kaftan, Juan B. Arellano, Ivana Kuta Smatanova, Alexander Dulebo, Jannette Carey, Katerina Hofbauerova, José L. Revuelta, M. Lapkouski, Olga Ettrichova, Vladimir Kopecky, Sergio González-Pérez, Zofie Sovova
Rok vydání: 2012
Předmět:
Models
Molecular
Protein Folding
Tridimensional structure
Photosystem II
Amino Acid Motifs
lcsh:Medicine
ComputingMilieux_LEGALASPECTSOFCOMPUTING
Crystal structure
Crystallography
X-Ray
Spectrum Analysis
Raman
Molecular Dynamics
Biochemistry
Biophysics Simulations
Protein Structure
Secondary
Crystal
Molecular dynamics
Protein structure
Computational Chemistry
Spinacia oleracea
Photosynthesis
lcsh:Science
Plant Proteins
Multidisciplinary
Chemistry
Plant Biochemistry
Physics
symbols
Molecular Mechanics
Protein crystallization
Research Article
Raman Spectroscopy
Protein Structure
Absorption spectroscopy
Molecular Sequence Data
Biophysics
Protein Chemistry
X-ray
symbols.namesake
Amino Acid Sequence
Protein Interactions
Biology
PsbP
lcsh:R
Photosystem II Protein Complex
Proteins
Hydrogen Bonding
Protein Structure
Tertiary
Crystallography
lcsh:Q
Raman spectroscopy
Zdroj: PLoS ONE
PLoS ONE, Vol 7, Iss 10, p e46694 (2012)
Digital.CSIC. Repositorio Institucional del CSIC
instname
ISSN: 1932-6203
6138-8971
Popis: This is an open-access article distributed under the terms of the Creative Commons Attribution License.-- et al.
Raman microscopy permits structural analysis of protein crystals in situ in hanging drops, allowing for comparison with Raman measurements in solution. Nevertheless, the two methods sometimes reveal subtle differences in structure that are often ascribed to the water layer surrounding the protein. The novel method of drop-coating deposition Raman spectropscopy (DCDR) exploits an intermediate phase that, although nominally “dry,” has been shown to preserve protein structural features present in solution. The potential of this new approach to bridge the structural gap between proteins in solution and in crystals is explored here with extrinsic protein PsbP of photosystem II from Spinacia oleracea. In the high-resolution (1.98 Å) x-ray crystal structure of PsbP reported here, several segments of the protein chain are present but unresolved. Analysis of the three kinds of Raman spectra of PsbP suggests that most of the subtle differences can indeed be attributed to the water envelope, which is shown here to have a similar Raman intensity in glassy and crystal states. Using molecular dynamics simulations cross-validated by Raman solution data, two unresolved segments of the PsbP crystal structure were modeled as loops, and the amino terminus was inferred to contain an additional beta segment. The complete PsbP structure was compared with that of the PsbP-like protein CyanoP, which plays a more peripheral role in photosystem II function. The comparison suggests possible interaction surfaces of PsbP with higher-plant photosystem II. This work provides the first complete structural picture of this key protein, and it represents the first systematic comparison of Raman data from solution, glassy, and crystalline states of a protein.
Support by the Academy of Sciences of the Czech Republic (RVO: 61388971, AVOZ60870520), the Ministry of Education of the Czech Republic (MSM6007665808, ME09062, COST LD11011), the Czech Science Foundation (grant 203/08/0114 to RE), and the Grant Agency of the Academy of Sciences of the Czech Republic (number IAA608170901 to DK and AD, number KJB101120805 to VK and KH) is gratefully acknowledged. JLR and JBA thank the Spanish Ministerio de Ciencia e Innovación (reference numbers BIO2008-00194 and BF2007-68107-C02-02/BMC).
Databáze: OpenAIRE
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