2avf: Difference between revisions

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[[Image:2avf.gif|left|200px]]
{{Seed}}
[[Image:2avf.png|left|200px]]


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{{STRUCTURE_2avf|  PDB=2avf  |  SCENE=  }}  
{{STRUCTURE_2avf|  PDB=2avf  |  SCENE=  }}  


'''Crystal Structure of C-terminal Desundecapeptide Nitrite Reductase from Achromobacter cycloclastes'''
===Crystal Structure of C-terminal Desundecapeptide Nitrite Reductase from Achromobacter cycloclastes===




==Overview==
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Monoclinic crystal structure of C-terminal desundecapeptide nitrite reductase (NiRc-11) from Achromobacter cycloclastes was determined at 2.6A. NiRc-11 exists as a loose trimer in the crystal. Deletion of 11 residues eliminates all intersubunit hydrogen bonds mediated by the C-terminal tail. The rigid irregular coil 105-112, which constitutes part of the sidewall of the active site pocket, undergoes conformational changes and becomes highly flexible in NiRc-11. Correspondingly, the linker segments between the two copper sites 95-100 and 135-136 are partly relaxed in conformation, which leads to disrupted active site microenvironments responsible for the activity loss and spectral change of NiRc-11. Comparison with the native structure revealed a bulky residue Met331 fastened by hydrogen bonding, which may play a direct role in keeping the right copper site geometry by protruding its side chain against the irregular coil 105-112. Sequence alignment showed that the bulky residue is conserved at position 331, indicating an equal importance of C-terminal segment in other copper-containing nitrite reductases.
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{{ABSTRACT_PUBMED_16293231}}


==About this Structure==
==About this Structure==
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[[Category: Zhang, J P.]]
[[Category: Zhang, J P.]]
[[Category: Beta barrel trimer]]
[[Category: Beta barrel trimer]]
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