1frv: Difference between revisions
New page: left|200px<br /><applet load="1frv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frv, resolution 2.85Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1frv.gif|left|200px]]<br /><applet load="1frv" size=" | [[Image:1frv.gif|left|200px]]<br /><applet load="1frv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1frv, resolution 2.85Å" /> | caption="1frv, resolution 2.85Å" /> | ||
'''CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE'''<br /> | '''CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
The X-ray structure of the heterodimeric Ni-Fe hydrogenase from | The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 A resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The 28K subunit, which coordinates one [3Fe-4S] and two [4Fe-4S] clusters, contains an amino-terminal domain with similarities to the redox protein flavodoxin. The structure suggests plausible electron and proton transfer pathways. | ||
==About this Structure== | ==About this Structure== | ||
1FRV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] with NI, SF4, F3S and FEL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c3_hydrogenase Cytochrome-c3 hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.2.1 1.12.2.1] Full crystallographic information is available from [http:// | 1FRV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=F3S:'>F3S</scene> and <scene name='pdbligand=FEL:'>FEL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c3_hydrogenase Cytochrome-c3 hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.2.1 1.12.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Desulfovibrio gigas]] | [[Category: Desulfovibrio gigas]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Fontecilla-Camps, J | [[Category: Fontecilla-Camps, J C.]] | ||
[[Category: Frey, M.]] | [[Category: Frey, M.]] | ||
[[Category: Volbeda, A.]] | [[Category: Volbeda, A.]] | ||
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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 12:41:56 2008'' | ||
Revision as of 10:41, 21 February 2008
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CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE
Overview
The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 A resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The 28K subunit, which coordinates one [3Fe-4S] and two [4Fe-4S] clusters, contains an amino-terminal domain with similarities to the redox protein flavodoxin. The structure suggests plausible electron and proton transfer pathways.
About this Structure
1FRV is a Protein complex structure of sequences from Desulfovibrio gigas with NI, SF4, F3S and FEL as ligands. Active as Cytochrome-c3 hydrogenase, with EC number 1.12.2.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas., Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M, Fontecilla-Camps JC, Nature. 1995 Feb 16;373(6515):580-7. PMID:7854413
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