1psf

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'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF PSAE FROM THE CYANOBACTERIUM SYNECHOCOCCUS SP. STRAIN PCC 7002: A PHOTOSYSTEM I PROTEIN THAT SHOWS STRUCTURAL HOMOLOGY WITH SH3 DOMAINS'''<br />
'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF PSAE FROM THE CYANOBACTERIUM SYNECHOCOCCUS SP. STRAIN PCC 7002: A PHOTOSYSTEM I PROTEIN THAT SHOWS STRUCTURAL HOMOLOGY WITH SH3 DOMAINS'''<br />
==Overview==
==Overview==
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PsaE is a 69 amino acid polypeptide from photosystem I present on the, stromal side of the thylakoid membrane. The three-dimensional solution, structure of this protein from the cyanobacterium Synechococcus sp. strain, PCC 7002 was determined at pH 5.8 and room temperature using over 900, experimental restraints derived from two- and three-dimensional NMR, experiments. The structure is comprised of a well-defined five-stranded, beta-sheet with (+1, +1, +1, -4 alpha) topology. There is no helical, region except for a single turn of 3(10) helix between the beta D and beta, E strands. PsaE also exhibits a large unrestrained loop spanning residues, 42-56. A comparison to known protein structures revealed similarity with, the Src homology 3 (SH3) domain, a membrane-associated protein involved in, signal transduction in eukaryotes. The match is remarkable as 47 of the, alpha-carbons of PsaE can be superimposed onto those of the SH3 domain, from chicken brain alpha-spectrin with a root-mean-square deviation of 2.3, A. Although the amino acid sequences have low identity and the loops are, different in both proteins, the topology of the beta-sheet and the 3(10), turn is conserved. SH3 domains from other sources show a similar, structural homology. The structure of PsaE was used to suggest approaches, for elucidating its roles within photosystem I.
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PsaE is a 69 amino acid polypeptide from photosystem I present on the stromal side of the thylakoid membrane. The three-dimensional solution structure of this protein from the cyanobacterium Synechococcus sp. strain PCC 7002 was determined at pH 5.8 and room temperature using over 900 experimental restraints derived from two- and three-dimensional NMR experiments. The structure is comprised of a well-defined five-stranded beta-sheet with (+1, +1, +1, -4 alpha) topology. There is no helical region except for a single turn of 3(10) helix between the beta D and beta E strands. PsaE also exhibits a large unrestrained loop spanning residues 42-56. A comparison to known protein structures revealed similarity with the Src homology 3 (SH3) domain, a membrane-associated protein involved in signal transduction in eukaryotes. The match is remarkable as 47 of the alpha-carbons of PsaE can be superimposed onto those of the SH3 domain from chicken brain alpha-spectrin with a root-mean-square deviation of 2.3 A. Although the amino acid sequences have low identity and the loops are different in both proteins, the topology of the beta-sheet and the 3(10) turn is conserved. SH3 domains from other sources show a similar structural homology. The structure of PsaE was used to suggest approaches for elucidating its roles within photosystem I.
==About this Structure==
==About this Structure==
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1PSF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PSF OCA].
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1PSF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSF OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Synechococcus sp.]]
[[Category: Synechococcus sp.]]
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[[Category: Bryant, D.A.]]
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[[Category: Bryant, D A.]]
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[[Category: Falzone, C.J.]]
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[[Category: Falzone, C J.]]
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[[Category: Kao, Y.H.]]
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[[Category: Kao, Y H.]]
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[[Category: Lecomte, J.T.J.]]
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[[Category: Lecomte, J T.J.]]
[[Category: Zhao, J.]]
[[Category: Zhao, J.]]
[[Category: photosystem i]]
[[Category: photosystem i]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:03 2008''

Revision as of 12:32, 21 February 2008


1psf

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THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF PSAE FROM THE CYANOBACTERIUM SYNECHOCOCCUS SP. STRAIN PCC 7002: A PHOTOSYSTEM I PROTEIN THAT SHOWS STRUCTURAL HOMOLOGY WITH SH3 DOMAINS

Overview

PsaE is a 69 amino acid polypeptide from photosystem I present on the stromal side of the thylakoid membrane. The three-dimensional solution structure of this protein from the cyanobacterium Synechococcus sp. strain PCC 7002 was determined at pH 5.8 and room temperature using over 900 experimental restraints derived from two- and three-dimensional NMR experiments. The structure is comprised of a well-defined five-stranded beta-sheet with (+1, +1, +1, -4 alpha) topology. There is no helical region except for a single turn of 3(10) helix between the beta D and beta E strands. PsaE also exhibits a large unrestrained loop spanning residues 42-56. A comparison to known protein structures revealed similarity with the Src homology 3 (SH3) domain, a membrane-associated protein involved in signal transduction in eukaryotes. The match is remarkable as 47 of the alpha-carbons of PsaE can be superimposed onto those of the SH3 domain from chicken brain alpha-spectrin with a root-mean-square deviation of 2.3 A. Although the amino acid sequences have low identity and the loops are different in both proteins, the topology of the beta-sheet and the 3(10) turn is conserved. SH3 domains from other sources show a similar structural homology. The structure of PsaE was used to suggest approaches for elucidating its roles within photosystem I.

About this Structure

1PSF is a Single protein structure of sequence from Synechococcus sp.. Full crystallographic information is available from OCA.

Reference

Three-dimensional solution structure of PsaE from the cyanobacterium Synechococcus sp. strain PCC 7002, a photosystem I protein that shows structural homology with SH3 domains., Falzone CJ, Kao YH, Zhao J, Bryant DA, Lecomte JT, Biochemistry. 1994 May 24;33(20):6052-62. PMID:8193119

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