1dox

<StructureSection load='1dox' size='340' side='right'caption='[[1dox]], [[NMR_Ensembles_of_Models | 3 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1dox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>

[[https://www.uniprot.org/uniprot/FER_SYNY3 FER_SYNY3]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:7578051</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Synechocystis sp]]

[[Category: Andre, F]]

[[Category: Bottin, H]]

[[Category: Lelong, C]]

[[Category: Neumann, J M]]

[[Category: Setif, P]]

[[Category: Iron-sulfur protein]]