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1frd

From Proteopedia

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[[Image:1frd.gif|left|200px]]
 
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{{Structure
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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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|PDB= 1frd |SIZE=350|CAPTION= <scene name='initialview01'>1frd</scene>, resolution 1.7&Aring;
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<StructureSection load='1frd' size='340' side='right'caption='[[1frd]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>
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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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|ACTIVITY=
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1frd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frd OCA], [http://www.ebi.ac.uk/pdbsum/1frd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1frd RCSB]</span>
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== Function ==
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}}
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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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'''MOLECULAR STRUCTURE OF THE OXIDIZED, RECOMBINANT, HETEROCYST (2FE-2S) FERREDOXIN FROM ANABAENA 7120 DETERMINED TO 1.7 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Large Structures]]
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[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
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==About this Structure==
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[[Category: Chae YK]]
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1FRD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRD OCA].
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[[Category: Holden HM]]
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[[Category: Jacobson BL]]
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==Reference==
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[[Category: Markley JL]]
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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://www.ncbi.nlm.nih.gov/pubmed/8329401 8329401]
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[[Category: Rayment I]]
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[[Category: Anabaena sp.]]
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[[Category: Single protein]]
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[[Category: Chae, Y K.]]
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[[Category: Holden, H M.]]
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[[Category: Jacobson, B L.]]
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[[Category: Markley, J L.]]
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[[Category: Rayment, I.]]
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[[Category: electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:45 2008''
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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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