1doy: Difference between revisions

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[[Image:1doy.gif|left|200px]]
[[Image:1doy.gif|left|200px]]


{{Structure
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'''1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803'''
'''1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803'''
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[[Category: Neumann, J M.]]
[[Category: Neumann, J M.]]
[[Category: Setif, P.]]
[[Category: Setif, P.]]
[[Category: iron-sulfur protein]]
[[Category: Iron-sulfur protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:05:59 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:51 2008''

Revision as of 14:06, 2 May 2008

File:1doy.gif

Template:STRUCTURE 1doy

1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803


OverviewOverview

The [2Fe-2S] ferredoxin extracted from Synechocystis sp. PCC 6803 was studied by 1H and 15N nuclear magnetic resonance. Sequence-specific 1H and 15N assignment of amino acid residues far from the paramagnetic cluster (distance higher than 8 A) was performed. Interresidue NOE constraints have allowed the identification of several secondary structure elements: one beta sheet composed of four beta strands, one alpha helix, and two alpha helix turns. The analysis of interresidue NOEs suggests the existence of a disulfide bridge between the cysteine residues 18 and 85. Such a disulfide bridge has never been observed in plant-type ferredoxins. Structure modeling using the X-PLOR program was performed with or without assuming the existence of a disulfide bridge. As a result, two structure families were obtained with rms deviations of 2.2 A. Due to the lack of NOE connectivities resulting from the paramagnetic effect from the [2Fe-2S] cluster, the structures were not well resolved in the region surrounding the [2Fe-2S] cluster, at both extremities of the alpha helix and the C and N terminus segments. In contrast, when taken separately, the beta sheet and the alpha helix were well defined. This work is the first report of a structure model of a plant-type [2Fe-2S] Fd in solution.

About this StructureAbout this Structure

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

ReferenceReference

1H and 15N NMR sequential assignment, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803., Lelong C, Setif P, Bottin H, Andre F, Neumann JM, Biochemistry. 1995 Nov 7;34(44):14462-73. PMID:7578051 Page seeded by OCA on Fri May 2 14:05:59 2008

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