1fxa

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(Difference between revisions)

Revision as of 07:09, 24 March 2021

CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM ANABAENA 7120

Structural highlights

1fxa is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FER1_NOSS1] 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 PubMed

The molecular structure of the oxidized form of the [2Fe-2S] ferredoxin isolated from the cyanobacterium Anabaena species strain PCC 7120 has been determined by X-ray diffraction analysis to a nominal resolution of 2.5 A and refined to a crystallographic R factor of 18.7%. Crystals used in this investigation belong to the space group P2(1)2(1)2(1) with unit cell dimensions of a = 37.42 A, b = 38.12 A, and c = 147.12 A and two molecules in the asymmetric unit. The three-dimensional structure of this ferredoxin was solved by a method that combined X-ray data from one isomorphous heavy-atom derivative with noncrystallographic symmetry averaging and solvent flattening. As in other plant-type [2Fe-2S] ferredoxins, the iron-sulfur cluster is located toward the outer edge of the molecule, and the irons are tetrahedrally coordinated by both inorganic sulfurs and sulfurs provided by protein cysteine residues. The main secondary structural elements include four strands of beta-pleated sheet and three alpha-helical regions.

Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120.,Rypniewski WR, Breiter DR, Benning MM, Wesenberg G, Oh BH, Markley JL, Rayment I, Holden HM Biochemistry. 1991 Apr 30;30(17):4126-31. PMID:1902376^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rypniewski WR, Breiter DR, Benning MM, Wesenberg G, Oh BH, Markley JL, Rayment I, Holden HM. Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry. 1991 Apr 30;30(17):4126-31. PMID:1902376

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fxa"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fxa' size='340' side='right'caption='[[1fxa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fxa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FXA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fxa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FXA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxa OCA], [http://pdbe.org/1fxa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fxa RCSB], [http://www.ebi.ac.uk/pdbsum/1fxa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxa ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxa OCA], [https://pdbe.org/1fxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fxa RCSB], [https://www.ebi.ac.uk/pdbsum/1fxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxa ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
+[[https://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Ferredoxin|Ferredoxin]]
+*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 == References ==
 <references/>

1fxa

From Proteopedia

Revision as of 07:09, 24 March 2021

CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM ANABAENA 7120

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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