1rfk

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[[Image:1rfk.gif|left|200px]]
[[Image:1rfk.gif|left|200px]]
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{{Structure
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|PDB= 1rfk |SIZE=350|CAPTION= <scene name='initialview01'>1rfk</scene>, resolution 1.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1rfk", creates the "Structure Box" on the page.
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{{STRUCTURE_1rfk| PDB=1rfk | SCENE= }}
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|RELATEDENTRY=[[1qt9|1QT9]], [[4fxc|4FXC]], [[1off|1OFF]], [[1a70|1A70]]
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1rfk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rfk RCSB]</span>
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'''Crystal Structure of 2Fe2S Ferredoxin from Thermophilic Cyanobacterium Mastigocladus Laminosus'''
'''Crystal Structure of 2Fe2S Ferredoxin from Thermophilic Cyanobacterium Mastigocladus Laminosus'''
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[[Category: Livnah, O.]]
[[Category: Livnah, O.]]
[[Category: Nechushtai, R.]]
[[Category: Nechushtai, R.]]
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[[Category: ferredoxin]]
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[[Category: Ferredoxin]]
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[[Category: thermostability]]
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[[Category: Thermostability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:26:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:27:27 2008''
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Revision as of 04:26, 3 May 2008

Template:STRUCTURE 1rfk

Crystal Structure of 2Fe2S Ferredoxin from Thermophilic Cyanobacterium Mastigocladus Laminosus


Overview

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.

About this Structure

1RFK is a Single protein structure of sequence from Mastigocladus laminosus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 07:26:13 2008

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