2avf
Crystal Structure of C-terminal Desundecapeptide Nitrite Reductase from Achromobacter cycloclastes
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OverviewOverview
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.
About this StructureAbout this Structure
2AVF is a Single protein structure of sequence from Achromobacter cycloclastes with CU and CL as ligands. Active as Nitrite reductase (NO-forming), with EC number 1.7.2.1 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of C-terminal desundecapeptide nitrite reductase from Achromobacter cycloclastes., Li HT, Chang T, Chang WC, Chen CJ, Liu MY, Gui LL, Zhang JP, An XM, Chang WR, Biochem Biophys Res Commun. 2005 Dec 30;338(4):1935-42. Epub 2005 Nov 15. PMID:16293231
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