1feh
From Proteopedia
(New page: 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=" | + | [[Image:1feh.gif|left|200px]]<br /><applet load="1feh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1feh, resolution 1.8Å" /> | caption="1feh, resolution 1.8Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Lanzilotta, W N.]] |
| - | [[Category: Lemon, B | + | [[Category: Lemon, B J.]] |
| - | [[Category: Peters, J | + | [[Category: Peters, J W.]] |
| - | [[Category: Seefeldt, L | + | [[Category: Seefeldt, L C.]] |
[[Category: FES]] | [[Category: FES]] | ||
[[Category: HC1]] | [[Category: HC1]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:48 2008'' |
Revision as of 10:37, 21 February 2008
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FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM
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.
About this Structure
1FEH is a Single protein structure of sequence from Clostridium pasteurianum with , and as ligands. Active as Ferredoxin hydrogenase, with EC number 1.12.7.2 Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution., Peters JW, Lanzilotta WN, Lemon BJ, Seefeldt LC, Science. 1998 Dec 4;282(5395):1853-8. PMID:9836629
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