1aom
From Proteopedia
(New page: 200px<br /><applet load="1aom" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aom, resolution 1.8Å" /> '''SUBSTRATE AND PRODUCT...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1aom.jpg|left|200px]]<br /><applet load="1aom" size=" | + | [[Image:1aom.jpg|left|200px]]<br /><applet load="1aom" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1aom, resolution 1.8Å" /> | caption="1aom, resolution 1.8Å" /> | ||
'''SUBSTRATE AND PRODUCT BOUND TO CYTOCHROME CD1 NITRITE REDUCTASE'''<br /> | '''SUBSTRATE AND PRODUCT BOUND TO CYTOCHROME CD1 NITRITE REDUCTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome cd1 nitrite reductase catalyses the conversion of nitrite to | + | Cytochrome cd1 nitrite reductase catalyses the conversion of nitrite to nitric oxide in the nitrogen cycle. The crystal structure of the oxidized enzyme shows that the d1 haem iron of the active site is ligated by His/Tyr side chains, and the c haem iron is ligated by a His/His ligand pair. Here we show that both haems undergo re-ligation during catalysis. Upon reduction, the tyrosine ligand of the d1 haem is released to allow substrate binding. Concomitantly, a refolding of the cytochrome c domain takes place, resulting in an unexpected change of the c haem iron coordination from His 17/His 69 to Met106/His69. This step is similar to the last steps in the folding of cytochrome c. The changes must affect the redox potential of the haems, and suggest a mechanism by which internal electron transfer is regulated. Structures of reaction intermediates show how nitric oxide is formed and expelled from the active-site iron, as well as how both haems return to their starting coordination. These results show how redox energy can be switched into conformational energy within a haem protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1AOM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus] with DHE, 2NO, HEM and NO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1AOM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus] with <scene name='pdbligand=DHE:'>DHE</scene>, <scene name='pdbligand=2NO:'>2NO</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NO:'>NO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOM OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
| - | [[Category: Williams, P | + | [[Category: Williams, P A.]] |
[[Category: 2NO]] | [[Category: 2NO]] | ||
[[Category: DHE]] | [[Category: DHE]] | ||
| Line 23: | Line 23: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:51 2008'' |
Revision as of 09:46, 21 February 2008
|
SUBSTRATE AND PRODUCT BOUND TO CYTOCHROME CD1 NITRITE REDUCTASE
Overview
Cytochrome cd1 nitrite reductase catalyses the conversion of nitrite to nitric oxide in the nitrogen cycle. The crystal structure of the oxidized enzyme shows that the d1 haem iron of the active site is ligated by His/Tyr side chains, and the c haem iron is ligated by a His/His ligand pair. Here we show that both haems undergo re-ligation during catalysis. Upon reduction, the tyrosine ligand of the d1 haem is released to allow substrate binding. Concomitantly, a refolding of the cytochrome c domain takes place, resulting in an unexpected change of the c haem iron coordination from His 17/His 69 to Met106/His69. This step is similar to the last steps in the folding of cytochrome c. The changes must affect the redox potential of the haems, and suggest a mechanism by which internal electron transfer is regulated. Structures of reaction intermediates show how nitric oxide is formed and expelled from the active-site iron, as well as how both haems return to their starting coordination. These results show how redox energy can be switched into conformational energy within a haem protein.
About this Structure
1AOM is a Single protein structure of sequence from Paracoccus pantotrophus with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme., Williams PA, Fulop V, Garman EF, Saunders NF, Ferguson SJ, Hajdu J, Nature. 1997 Sep 25;389(6649):406-12. PMID:9311786
Page seeded by OCA on Thu Feb 21 11:46:51 2008
Categories: Paracoccus pantotrophus | Single protein | Fulop, V. | Williams, P A. | 2NO | DHE | HEM | NO | Enzyme | Nitrite reductase | Oxidoreductase
