1f37

<StructureSection load='1f37' size='340' side='right' caption='[[1f37]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[1f37]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F37 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1f37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f37 OCA], [http://pdbe.org/1f37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f37 RCSB], [http://www.ebi.ac.uk/pdbsum/1f37 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/FER2_AQUAE FER2_AQUAE]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f3/1f37_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The 2.3 A resolution crystal structure of a [2Fe-2S] cluster containing ferredoxin from Aquifex aeolicus reveals a thioredoxin-like fold that is novel among iron-sulfur proteins. The [2Fe-2S] cluster is located near the surface of the protein, at a site corresponding to that of the active-site disulfide bridge in thioredoxin. The four cysteine ligands are located near the ends of two surface loops. Two of these ligands can be substituted by non-native cysteine residues introduced throughout a stretch of the polypeptide chain that forms a protruding loop extending away from the cluster. The presence of homologs of this ferredoxin as components of more complex anaerobic and aerobic electron transfer systems indicates that this is a versatile fold for biological redox processes.

Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.,Yeh AP, Chatelet C, Soltis SM, Kuhn P, Meyer J, Rees DC J Mol Biol. 2000 Jul 14;300(3):587-95. PMID:10884354<ref>PMID:10884354</ref>

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

</div>

<div class="pdbe-citations 1f37" style="background-color:#fffaf0;"></div>

*[[Ferredoxin|Ferredoxin]]

[[Category: Aquifex aeolicus huber and stetter 2001]]

[[Category: Chatelet, C]]

[[Category: Kuhn, P]]

[[Category: Meyer, J]]

[[Category: Rees, D C]]

[[Category: Soltis, S M]]

[[Category: Yeh, A P]]

[[Category: Thioredoxin fold]]