1qdb: Difference between revisions

New page: left|200px<br /><applet load="1qdb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qdb, resolution 1.90Å" /> '''CYTOCHROME C NITRITE...
 
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[[Image:1qdb.jpg|left|200px]]<br /><applet load="1qdb" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1qdb.jpg|left|200px]]<br /><applet load="1qdb" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1qdb, resolution 1.90&Aring;" />
caption="1qdb, resolution 1.90&Aring;" />
'''CYTOCHROME C NITRITE REDUCTASE'''<br />
'''CYTOCHROME C NITRITE REDUCTASE'''<br />


==Overview==
==Overview==
The enzyme cytochrome c nitrite reductase catalyses the six-electron, reduction of nitrite to ammonia as one of the key steps in the biological, nitrogen cycle, where it participates in the anaerobic energy metabolism, of dissimilatory nitrate ammonification. Here we report on the crystal, structure of this enzyme from the microorganism Sulfurospirillum, deleyianum, which we solved by multiwavelength anomalous dispersion, methods. We propose a reaction scheme for the transformation of nitrite, based on structural and spectroscopic information. Cytochrome c nitrite, reductase is a functional dimer, with 10 close-packed haem groups of type, c and an unusual lysine-coordinated high-spin haem at the active site. By, comparing the haem arrangement of this nitrite reductase with that of, other multihaem cytochromes, we have been able to identify a family of, proteins in which the orientation of haem groups is conserved whereas, structure and function are not.
The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key steps in the biological nitrogen cycle, where it participates in the anaerobic energy metabolism of dissimilatory nitrate ammonification. Here we report on the crystal structure of this enzyme from the microorganism Sulfurospirillum deleyianum, which we solved by multiwavelength anomalous dispersion methods. We propose a reaction scheme for the transformation of nitrite based on structural and spectroscopic information. Cytochrome c nitrite reductase is a functional dimer, with 10 close-packed haem groups of type c and an unusual lysine-coordinated high-spin haem at the active site. By comparing the haem arrangement of this nitrite reductase with that of other multihaem cytochromes, we have been able to identify a family of proteins in which the orientation of haem groups is conserved whereas structure and function are not.


==About this Structure==
==About this Structure==
1QDB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfurospirillum_deleyianum Sulfurospirillum deleyianum] with CA, SO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QDB OCA].  
1QDB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfurospirillum_deleyianum Sulfurospirillum deleyianum] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDB OCA].  


==Reference==
==Reference==
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[[Category: Einsle, O.]]
[[Category: Einsle, O.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Kroneck, P.M.H.]]
[[Category: Kroneck, P M.H.]]
[[Category: Messerschmidt, A.]]
[[Category: Messerschmidt, A.]]
[[Category: Stach, P.]]
[[Category: Stach, P.]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


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