1frd

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(New page: 200px<br /><applet load="1frd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frd, resolution 1.7&Aring;" /> '''MOLECULAR STRUCTURE O...)
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[[Image:1frd.gif|left|200px]]<br /><applet load="1frd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1frd, resolution 1.7&Aring;" />
 
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'''MOLECULAR STRUCTURE OF THE OXIDIZED, RECOMBINANT, HETEROCYST (2FE-2S) FERREDOXIN FROM ANABAENA 7120 DETERMINED TO 1.7 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==MOLECULAR STRUCTURE OF THE OXIDIZED, RECOMBINANT, HETEROCYST (2FE-2S) FERREDOXIN FROM ANABAENA 7120 DETERMINED TO 1.7 ANGSTROMS RESOLUTION==
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The [2Fe-2S] ferredoxin produced in the heterocyst cells of Anabaena 7120, plays a key role in nitrogen fixation, where it serves as an electron, acceptor from various sources and an electron donor to nitrogenase. The, three-dimensional structure of this ferredoxin has now been determined and, refined to a crystallographic R value of 16.7%, with all measured X-ray, data from 30.0 to 1.7 A. The molecular motif of this ferredoxin is similar, to that of other plant-type ferredoxins with the iron-sulfur cluster, located toward the outer edge of the molecule and the irons tetrahedrally, coordinated by both inorganic sulfurs and sulfurs provided by protein, cysteinyl residues. The overall secondary structure of the molecule, consists of seven strands of beta-pleated sheet, two alpha-helices, and, seven type I turns. It is of special interest that 4 of the 22 amino acid, positions thought to be absolutely conserved in nonhalophilic ferredoxins, are different in the heterocyst form of the protein. Three of these, positions are located in the metal-cluster binding loop.
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<StructureSection load='1frd' size='340' side='right'caption='[[1frd]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1frd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1frd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frd OCA], [https://pdbe.org/1frd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frd RCSB], [https://www.ebi.ac.uk/pdbsum/1frd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FERH_NOSS1 FERH_NOSS1] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Donates electrons to the nitrogenase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/1frd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1frd ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRD OCA].
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution., Jacobson BL, Chae YK, Markley JL, Rayment I, Holden HM, Biochemistry. 1993 Jul 6;32(26):6788-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8329401 8329401]
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[[Category: Large Structures]]
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[[Category: Anabaena sp.]]
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[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
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[[Category: Single protein]]
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[[Category: Chae YK]]
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[[Category: Chae, Y.K.]]
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[[Category: Holden HM]]
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[[Category: Holden, H.M.]]
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[[Category: Jacobson BL]]
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[[Category: Jacobson, B.L.]]
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[[Category: Markley JL]]
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[[Category: Markley, J.L.]]
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[[Category: Rayment I]]
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[[Category: Rayment, I.]]
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[[Category: FES]]
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[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:11:19 2007''
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Current revision

MOLECULAR STRUCTURE OF THE OXIDIZED, RECOMBINANT, HETEROCYST (2FE-2S) FERREDOXIN FROM ANABAENA 7120 DETERMINED TO 1.7 ANGSTROMS RESOLUTION

PDB ID 1frd

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