1baw

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==Overview==
==Overview==
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The crystal structure of the 'blue' copper protein plastocyanin from the, cyanobacterium Phormidium laminosum has been solved and refined using 2.8, A X--ray data. P. laminosum plastocyanin crystallizes in space group, P43212 with unit-cell dimensions a = 86.57, c = 91.47 A and with three, protein molecules per asymmetric unit. The final residual R is 19.9%. The, structure was solved using molecular replacement with a search model based, on the crystal structure of a close homologue, Anabaena variabilis, plastocyanin (66% sequence identity). The molecule of P. laminosum, plastocyanin has 105 amino-acid residues. The single Cu atom is, coordinated by the same residues - two histidines, a cysteine and a, methionine - as in other plastocyanins. In the crystal structure, the, three molecules of the asymmetric unit are related by a, non-crystallographic threefold axis. A Zn atom lies between each pair of, neighbouring molecules in this ensemble, being coordinated by a surface, histidine residue of one molecule and by two aspartates of the other.
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The crystal structure of the 'blue' copper protein plastocyanin from the cyanobacterium Phormidium laminosum has been solved and refined using 2.8 A X--ray data. P. laminosum plastocyanin crystallizes in space group P43212 with unit-cell dimensions a = 86.57, c = 91.47 A and with three protein molecules per asymmetric unit. The final residual R is 19.9%. The structure was solved using molecular replacement with a search model based on the crystal structure of a close homologue, Anabaena variabilis plastocyanin (66% sequence identity). The molecule of P. laminosum plastocyanin has 105 amino-acid residues. The single Cu atom is coordinated by the same residues - two histidines, a cysteine and a methionine - as in other plastocyanins. In the crystal structure, the three molecules of the asymmetric unit are related by a non-crystallographic threefold axis. A Zn atom lies between each pair of neighbouring molecules in this ensemble, being coordinated by a surface histidine residue of one molecule and by two aspartates of the other.
==About this Structure==
==About this Structure==
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[[Category: Phormidium laminosum]]
[[Category: Phormidium laminosum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bendall, D.S.]]
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[[Category: Bendall, D S.]]
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[[Category: Bond, C.S.]]
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[[Category: Bond, C S.]]
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[[Category: Freeman, H.C.]]
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[[Category: Freeman, H C.]]
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[[Category: Guss, J.M.]]
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[[Category: Guss, J M.]]
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[[Category: Howe, C.J.]]
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[[Category: Howe, C J.]]
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[[Category: Wagner, M.J.]]
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[[Category: Wagner, M J.]]
[[Category: CU]]
[[Category: CU]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: electron transfer]]
[[Category: electron transfer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:32:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:20 2008''

Revision as of 09:53, 21 February 2008


1baw, resolution 2.8Å

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PLASTOCYANIN FROM PHORMIDIUM LAMINOSUM

Overview

The crystal structure of the 'blue' copper protein plastocyanin from the cyanobacterium Phormidium laminosum has been solved and refined using 2.8 A X--ray data. P. laminosum plastocyanin crystallizes in space group P43212 with unit-cell dimensions a = 86.57, c = 91.47 A and with three protein molecules per asymmetric unit. The final residual R is 19.9%. The structure was solved using molecular replacement with a search model based on the crystal structure of a close homologue, Anabaena variabilis plastocyanin (66% sequence identity). The molecule of P. laminosum plastocyanin has 105 amino-acid residues. The single Cu atom is coordinated by the same residues - two histidines, a cysteine and a methionine - as in other plastocyanins. In the crystal structure, the three molecules of the asymmetric unit are related by a non-crystallographic threefold axis. A Zn atom lies between each pair of neighbouring molecules in this ensemble, being coordinated by a surface histidine residue of one molecule and by two aspartates of the other.

About this Structure

1BAW is a Single protein structure of sequence from Phormidium laminosum with and as ligands. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.

Reference

The structure of plastocyanin from the cyanobacterium Phormidium laminosum., Bond CS, Bendall DS, Freeman HC, Guss JM, Howe CJ, Wagner MJ, Wilce MC, Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):414-21. PMID:10089349

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