1rfk

<table><tr><td colspan='2'>[[1rfk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mastigocladus_laminosus Mastigocladus laminosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RFK 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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qt9|1qt9]], [[4fxc|4fxc]], [[1off|1off]], [[1a70|1a70]]</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=1rfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfk OCA], [http://pdbe.org/1rfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rfk RCSB], [http://www.ebi.ac.uk/pdbsum/1rfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rfk ProSAT]</span></td></tr>

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

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== Publication Abstract from PubMed ==

Plant-type ferredoxins (Fds) carry a single [2Fe-2S] cluster and serve as electron acceptors of photosystem I (PSI). The ferredoxin from the thermophilic cyanobacterium Mastigocladus laminosus displays optimal activity at 65 degrees C. In order to reveal the molecular factors that confer thermostability, the crystal structure of M.laminosus Fd (mFd) was determined to 1.25 A resolution and subsequently analyzed in comparison with four similar plant-type mesophilic ferredoxins. The topologies of the plant-type ferredoxins are similar, yet two structural determinants were identified that may account for differences in thermostability, a salt bridge network in the C-terminal region, and the flexible L1,2 loop that increases hydrophobic accessible surface area. These conclusions were verified by three mutations, i.e. substitution of L1,2 into a rigid beta-turn ((Delta)L1,2) and two point mutations (E90S and E96S) that disrupt the salt bridge network at the C-terminal region. All three mutants have shown reduced electron transfer (ET) capabilities and [2Fe-2S] stability at high temperatures in comparison to the wild-type mFd. The results have also provided new insights into the involvement of the L1,2 loop in the Fd interactions with its electron donor, the PSI complex.

Structural basis for the thermostability of ferredoxin from the cyanobacterium Mastigocladus laminosus.,Fish A, Danieli T, Ohad I, Nechushtai R, Livnah O J Mol Biol. 2005 Jul 15;350(3):599-608. PMID:15961101<ref>PMID:15961101</ref>

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

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

== References ==

<references/>

[[Category: Fish, A]]

[[Category: Livnah, O]]

[[Category: Nechushtai, R]]

[[Category: Thermostability]]