1ewy: Difference between revisions
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<StructureSection load='1ewy' size='340' side='right'caption='[[1ewy]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='1ewy' size='340' side='right'caption='[[1ewy]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ewy]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ewy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._pcc_7119 Nostoc sp. pcc 7119]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EWY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qt9|1qt9]], [[1que|1que]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qt9|1qt9]], [[1que|1que]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ewy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ewy OCA], [https://pdbe.org/1ewy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ewy RCSB], [https://www.ebi.ac.uk/pdbsum/1ewy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ewy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/FER1_NOSSO FER1_NOSSO]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 12:43, 21 July 2021
ANABAENA PCC7119 FERREDOXIN:FERREDOXIN-NADP+-REDUCTASE COMPLEXANABAENA PCC7119 FERREDOXIN:FERREDOXIN-NADP+-REDUCTASE COMPLEX
Structural highlights
Function[FER1_NOSSO] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFerredoxin-NADP(+) reductase (FNR) and its physiological electron donor ferredoxin (Fd) from the cyanobacterium Anabaena PCC7119 have been co-crystallized. The unit-cell parameters are a = b = 63.72, c = 158.02 A and the space group is P2(1)2(1)2(1). The crystal structure has been solved with 2.4 A resolution synchrotron data by molecular replacement, anomalous dispersion and R(min) search methods. For the computations, the crystal was treated as a merohedral twin. The asymmetric unit contains two FNR molecules and one ferredoxin molecule. The packing of the FNR molecules displays a nearly tetragonal symmetry (space group P4(3)2(1)2), whereas the ferredoxin arrangement is orthorhombic. This study provides the first crystallographic model of a dissociable complex between FNR and Fd. Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule.,Morales R, Kachalova G, Vellieux F, Charon MH, Frey M Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1408-12. PMID:11053838[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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