1doy: Difference between revisions
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'''1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803''' | {{Structure | ||
|PDB= 1doy |SIZE=350|CAPTION= <scene name='initialview01'>1doy</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DOY is a [ | 1DOY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOY OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7578051 7578051] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
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[[Category: iron-sulfur protein]] | [[Category: iron-sulfur protein]] | ||
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Revision as of 11:41, 20 March 2008
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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
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