1qt9
From Proteopedia
(New page: 200px<br /><applet load="1qt9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qt9, resolution 1.30Å" /> '''OXIDIZED [2FE-2S] FE...) |
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| - | [[Image:1qt9.jpg|left|200px]]<br /><applet load="1qt9" size=" | + | [[Image:1qt9.jpg|left|200px]]<br /><applet load="1qt9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qt9, resolution 1.30Å" /> | caption="1qt9, resolution 1.30Å" /> | ||
'''OXIDIZED [2FE-2S] FERREDOXIN FROM ANABAENA PCC7119'''<br /> | '''OXIDIZED [2FE-2S] FERREDOXIN FROM ANABAENA PCC7119'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The chemical sequence of the [2Fe-2S] ferredoxin from the cyanobacterium | + | The chemical sequence of the [2Fe-2S] ferredoxin from the cyanobacterium AnabaenaPCC7119 (Fd7119) and its high-resolution X-ray structures in the oxidized and reduced states have been determined. The Fd7119 sequence is identical to that of the ferredoxin from the PCC7120 strain (Fd7120). X-ray diffraction data were collected at 100 K with an oxidized trigonal Fd7119 crystal, at 1.3 A resolution, and with an orthorhombic crystal, previously reduced with dithionite and flash frozen under anaerobic conditions, at 1.17 A resolution. The two molecular models were determined by molecular replacement with the [2Fe-2S] ferredoxin from the strain PCC7120 (Rypniewski, W. R., Breiter, D. R., Benning, M. M., Wesenberg, G., Oh, B.-H., Markley, J. L., Rayment, I., and Holden, H. M. (1991) Biochemistry 30, 4126-4131.) The final R-factors are 0. 140 (for the reduced crystal) and 0.138 (for the oxidized crystal). The [2Fe-2S] cluster appears as a significantly distorted lozenge in the reduced and oxidized redox states. The major conformational difference between the two redox forms concerns the peptide bond linking Cys46 and Ser47 which points its carbonyl oxygen away from the [2Fe-2S] cluster ("CO out") in the reduced molecule and toward it ("CO in") in the oxidized one. The "CO out" conformation could be the signature of the reduction of the iron atom Fe1, which is close to the molecular surface. Superposition of the three crystallographically independent molecules shows that the putative recognition site with the physiological partner (FNR) involves charged, hydrophobic residues and invariant water molecules. |
==About this Structure== | ==About this Structure== | ||
| - | 1QT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QT9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Anabaena sp.]] | [[Category: Anabaena sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chron, M | + | [[Category: Chron, M H.]] |
[[Category: Frey, M.]] | [[Category: Frey, M.]] | ||
[[Category: Hudry-Clergeon, G.]] | [[Category: Hudry-Clergeon, G.]] | ||
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[[Category: oxidized ferredoxin]] | [[Category: oxidized ferredoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:28 2008'' |
Revision as of 12:43, 21 February 2008
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OXIDIZED [2FE-2S] FERREDOXIN FROM ANABAENA PCC7119
Overview
The chemical sequence of the [2Fe-2S] ferredoxin from the cyanobacterium AnabaenaPCC7119 (Fd7119) and its high-resolution X-ray structures in the oxidized and reduced states have been determined. The Fd7119 sequence is identical to that of the ferredoxin from the PCC7120 strain (Fd7120). X-ray diffraction data were collected at 100 K with an oxidized trigonal Fd7119 crystal, at 1.3 A resolution, and with an orthorhombic crystal, previously reduced with dithionite and flash frozen under anaerobic conditions, at 1.17 A resolution. The two molecular models were determined by molecular replacement with the [2Fe-2S] ferredoxin from the strain PCC7120 (Rypniewski, W. R., Breiter, D. R., Benning, M. M., Wesenberg, G., Oh, B.-H., Markley, J. L., Rayment, I., and Holden, H. M. (1991) Biochemistry 30, 4126-4131.) The final R-factors are 0. 140 (for the reduced crystal) and 0.138 (for the oxidized crystal). The [2Fe-2S] cluster appears as a significantly distorted lozenge in the reduced and oxidized redox states. The major conformational difference between the two redox forms concerns the peptide bond linking Cys46 and Ser47 which points its carbonyl oxygen away from the [2Fe-2S] cluster ("CO out") in the reduced molecule and toward it ("CO in") in the oxidized one. The "CO out" conformation could be the signature of the reduction of the iron atom Fe1, which is close to the molecular surface. Superposition of the three crystallographically independent molecules shows that the putative recognition site with the physiological partner (FNR) involves charged, hydrophobic residues and invariant water molecules.
About this Structure
1QT9 is a Single protein structure of sequence from Anabaena sp. with as ligand. Full crystallographic information is available from OCA.
Reference
Refined X-ray structures of the oxidized, at 1.3 A, and reduced, at 1.17 A, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes., Morales R, Charon MH, Hudry-Clergeon G, Petillot Y, Norager S, Medina M, Frey M, Biochemistry. 1999 Nov 30;38(48):15764-73. PMID:10625442
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