2AVF

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

Summary for 2AVF

• Entry DOI: 10.2210/pdb2avf/pdb
• Related: 1RZP 1RZQ
• Descriptor: Copper-containing nitrite reductase, COPPER (II) ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: beta barrel trimer, oxidoreductase
• Biological source: Achromobacter cycloclastes
• Cellular location: Periplasm: P25006
• Total number of polymer chains: 6
• Total formula weight: 216455.50

Authors

Li, H.T.,Chang, T.,Chang, W.C.,Chen, C.J.,Liu, M.Y.,Gui, L.L.,Zhang, J.P.,An, X.M.,Chang, W.R. (deposition date: 2005-08-30, release date: 2005-12-20, Last modification date: 2024-03-13)

Primary citation

Li, H.T.,Chang, T.,Chang, W.C.,Chen, C.J.,Liu, M.Y.,Gui, L.L.,Zhang, J.P.,An, X.M.,Chang, W.R.
Crystal structure of C-terminal desundecapeptide nitrite reductase from Achromobacter cycloclastes
Biochem.Biophys.Res.Commun., 338:1935-1942, 2005

PubMed Abstract: 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.

PubMed: 16293231
DOI: 10.1016/j.bbrc.2005.09.199

Experimental method

X-RAY DIFFRACTION (2.6 Å)