1dox

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[[Image:1dox.jpg|left|200px]]<br /><applet load="1dox" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dox.jpg|left|200px]]
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caption="1dox" />
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'''1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803'''<br />
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{{Structure
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|PDB= 1dox |SIZE=350|CAPTION= <scene name='initialview01'>1dox</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DOX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOX OCA].
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1DOX 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=1DOX OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7578051 7578051]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:03 2008''

Revision as of 08:42, 20 March 2008


PDB ID 1dox

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


Overview

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 Structure

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

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:7578051

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