1feh: Difference between revisions

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New page: left|200px<br /><applet load="1feh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1feh, resolution 1.8Å" /> '''FE-ONLY HYDROGENASE F...
 
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[[Image:1feh.gif|left|200px]]<br /><applet load="1feh" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1feh.gif|left|200px]]<br /><applet load="1feh" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1feh, resolution 1.8&Aring;" />
caption="1feh, resolution 1.8&Aring;" />
'''FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM'''<br />
'''FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM'''<br />


==Overview==
==Overview==
A three-dimensional structure for the monomeric iron-containing, hydrogenase (CpI) from Clostridium pasteurianum was determined to 1.8, angstrom resolution by x-ray crystallography using multiwavelength, anomalous dispersion (MAD) phasing. CpI, an enzyme that catalyzes the, two-electron reduction of two protons to yield dihydrogen, was found to, contain 20 gram atoms of iron per mole of protein, arranged into five, distinct [Fe-S] clusters. The probable active-site cluster, previously, termed the H-cluster, was found to be an unexpected arrangement of six, iron atoms existing as a [4Fe-4S] cubane subcluster covalently bridged by, a cysteinate thiol to a [2Fe] subcluster. The iron atoms of the [2Fe], subcluster both exist with an octahedral coordination geometry and are, bridged to each other by three non-protein atoms, assigned as two sulfide, atoms and one carbonyl or cyanide molecule. This structure provides, insights into the mechanism of biological hydrogen activation and has, broader implications for [Fe-S] cluster structure and function in, biological systems.
A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined to 1.8 angstrom resolution by x-ray crystallography using multiwavelength anomalous dispersion (MAD) phasing. CpI, an enzyme that catalyzes the two-electron reduction of two protons to yield dihydrogen, was found to contain 20 gram atoms of iron per mole of protein, arranged into five distinct [Fe-S] clusters. The probable active-site cluster, previously termed the H-cluster, was found to be an unexpected arrangement of six iron atoms existing as a [4Fe-4S] cubane subcluster covalently bridged by a cysteinate thiol to a [2Fe] subcluster. The iron atoms of the [2Fe] subcluster both exist with an octahedral coordination geometry and are bridged to each other by three non-protein atoms, assigned as two sulfide atoms and one carbonyl or cyanide molecule. This structure provides insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems.


==About this Structure==
==About this Structure==
1FEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with HC1, SF4 and FES as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FEH OCA].  
1FEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with <scene name='pdbligand=HC1:'>HC1</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FEH OCA].  


==Reference==
==Reference==
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[[Category: Ferredoxin hydrogenase]]
[[Category: Ferredoxin hydrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lanzilotta, W.N.]]
[[Category: Lanzilotta, W N.]]
[[Category: Lemon, B.J.]]
[[Category: Lemon, B J.]]
[[Category: Peters, J.W.]]
[[Category: Peters, J W.]]
[[Category: Seefeldt, L.C.]]
[[Category: Seefeldt, L C.]]
[[Category: FES]]
[[Category: FES]]
[[Category: HC1]]
[[Category: HC1]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:51:14 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:48 2008''