Crystal structure of oxygen-evolving photosystem II from <i>Thermosynechococcus vulcanus</i> at 3.7-Å resolution

Nobuo Kamiya1, Jian‐Ren Shen1
1RIKEN, Harima Institute/Spring-8, Kouto 1-1-1, Mikazuki-cho, Sayou-gun, Hyogo 679-5148, Japan

Tóm tắt

Photosystem II (PSII) is a multisubunit membrane protein complex performing light-induced electron transfer and water-splitting reactions, leading to the formation of molecular oxygen. The first crystal structure of PSII from a thermophilic cyanobacterium Thermosynechococcus elongatus was reported recently [Zouni, A., Witt, H. T., Kern, J., Fromme, P., Krauss, N., Saenger, W. & Orth, P. (2001) Nature 409, 739–743)] at 3.8-Å resolution. To analyze the PSII structure in more detail, we have obtained the crystal structure of PSII from another thermophilic cyanobacterium, Thermosynechococcus vulcanus , at 3.7-Å resolution. The present structure was built on the basis of the sequences of PSII large subunits D1, D2, CP47, and CP43; extrinsic 33- and 12-kDa proteins and cytochrome c 550; and several low molecular mass subunits, among which the structure of the 12-kDa protein was not reported previously. This yielded much information concerning the molecular interactions within this large protein complex. We also show the arrangement of chlorophylls and cofactors, including two β-carotenes recently identified in a region close to the reaction center, which provided important clues to the secondary electron transfer pathways around the reaction center. Furthermore, possible ligands for the Mn-cluster were determined. In particular, the C terminus of D1 polypeptide was shown to be connected to the Mn cluster directly. The structural information obtained here provides important insights into the mechanism of PSII reactions.

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Tài liệu tham khảo

B Hankamer, J Barber, E J Boekema Annu Rev Plant Physiol Plant Mol Biol 48, 641–647 (1997).

R J Debus Metal Ions in Biological Systems, ed A Sigel (Dekker, New York) 37, 657–711 (2000).

J Barber Curr Opin Struct Biol 12, 523–530 (2002).

K-H Rhee, E P Morris, D Zheleva, B Hankamer, W Kuhlbrandt, J Barber Nature 389, 522–526 (1997).

K-H Rhee, E P Morris, J Barber, W Kuhlbrandt Nature 396, 283–286 (1998).

A Zouni, R Jordan, E Schlodder, P Fromme, H T Witt Biochim Biophys Acta 1457, 103–105 (2000).

H Kuhl, J Kruip, A Seidler, A Krieger-Liszkay, M Bünker, D Bald, A J Scheidig, M Rögner J Biol Chem 275, 20652–20659 (2000).

J-R Shen, N Kamiya Biochemistry 39, 14739–14744 (2000).

A Zouni, H-T Witt, J Kern, P Fromme, N Krauss, W Saenger, P Orth Nature 409, 739–743 (2001).

J-R Shen, M Ikeuchi, Y Inoue FEBS Lett 301, 145–149 (1992).

J-R Shen, Y Inoue Biochemistry 32, 1825–1832 (1993).

M Kawamoto, Y Kawano, N Kamiya Nucl Instr Methods A 467–468, 1375–1379 (2001).

I Steller, B Bolotovsky, M G Rossmann J Appl Crystallogr D 30, 1036–1040 (1997).

Acta Crystallogr D 50, 760–763 (1994).

E de la Fortelle, G Bricogne Methods Enzymol 276, 472–494 (1997).

Y Nakamura, T Kaneko, S Sato, M Ikeuchi, H Katoh, S Sasamoto, A Watanabe, M Iriguchi, K Kawashima, T Kimura, et al. DNA Res 9, 123–130 (2002).

G N Murshudov, A A Vagin, E J Dodson Acta Crystallogr D 53, 240–255 (1997).

P J Kraulis J Appl Crystallogr 24, 946–950 (1991).

E A Merritt, D J Bacon Methods Enzymol 277, 505–524 (1997).

J Deisenhofer, H Michel Annu Rev Cell Biol 7, 1–23 (1991).

H Michel, J Deisenhofer Biochemistry 27, 1–7 (1988).

J P M Schelvis, P I van Noort, T J Aartsma, H J van Gorkom Biochim Biophys Acta 1184, 242–250 (1994).

D H Stewart, A Cua, D A Chisholm, B Diner, D F Bocian, G W Brudvig Biochemistry 37, 10040–10046 (1998).

M T Lince, W F J Vermaas Eur J Biochem 256, 595–602 (1998).

H G Johnston, J Wang, S V Ruffle, R T Sayre, T L Gustafson J Phys Chem B 104, 4777–4781 (2000).

P Jordan, P Fromme, H T Witt, O Klukas, W Saenger, N Krauss Nature 411, 909–917 (2001).

L X Shi, S, J Kim, A Marchant, C Robinson, W P Schroder Plant Mol Biol 40, 737–744 (1999).

C Büchel, E Morris, E Orlova, J Barber J Mol Biol 312, 371–379 (2001).

T Tomo, I Enami, K Satoh FEBS Lett 323, 15–18 (1993).

Sugimoto I. & Takahashi Y. (2001) PS2001 Proceedings 12th International Congress on Photosynthesis S5-033 [CSIRO Australia (www.csiro.au/index.asp)].

E J Summer, V H Schmid, B U Bruns, G W Schmidt Plant Physiol 113, 1359–1368 (1997).

D Zheleva, J Sharma, M Panico, H R Morris, J Barber J Biol Chem 273, 16122–16127 (1998).

B Hankamer, E P Morris, J Nield, C Gerle, J Barber J Struct Biol 135, 262–269 (2001).

Q Xu, J Nelson, T M Bricker Biochim Biophys Acta 1188, 427–431 (1994).

A Ahmed, H A Tajmir-Riahi, R Carpentier FEBS Lett 363, 65–68 (1995).

J Vogt, G E Schulz Struct Folding Des 7, 1301–1309 (1999).

A Pautsch, G E Schulz J Mol Biol 298, 273–282 (2000).

F Pazos, P Heredia, A Valencia, J de las Rivas Proteins Struct Funct Genet 45, 372–381 (2001).

J Nield, M Balsera, J de las Rivas, J Barber J Biol Chem 277, 15006–15012 (2002).

J S Vrettos, M J Reifler, O Kievit, K V Lakshmi, J C de Paula, G W Brudvig J Biol Inorg Chem 6, 708–716 (2001).

M R Sawaya, D W Krogmann, A Serag, K K Ho, T O Yeates, C A Kerfeld Biochemistry 40, 9215–9225 (2001).

A Seidler Biochim Biophys Acta 1277, 36–60 (1996).

T M Bricker, L K Frankel Photosynth Res 72, 131–146 (2002).

S Vasil'ev, P Orth, A Zouni, T G Owens, D Bruce Proc Natl Acad Sci USA 98, 8602–8607 (2001).

J Barber, M D Archer J Photochem Photobiol A 142, 97–106 (2001).

B A Diner, F Rappaport Annu Rev Plant Biol 53, 551–580 (2002).

G E Bialek-Bylka, T Tomo, K Satoh, Y Koyama FEBS Lett 363, 137–140 (1995).

C A Tracewell, J S Vrettos, J A Bautista, H A Frank, G W Brudvig Arch Biochem Biophys 385, 61–69 (2001).

W R Newell, H van Amerongen, J Barber, R van Grondelle Biochim Biophys Acta 1057, 232–238 (1991).

R J Debus Biochim Biophys Acta 1503, 164–186 (2001).

C Preston, M Seibert Biochemistry 30, 9625–9633 (1991).