1RZQ

Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0

Summary for 1RZQ

• Entry DOI: 10.2210/pdb1rzq/pdb
• Related: 1RZP
• Descriptor: Copper-containing nitrite reductase, COPPER (II) ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: denitrification, residue deletion, ph profile, greek key beta barrel, oxidoreductase
• Biological source: Achromobacter cycloclastes
• Cellular location: Periplasm: P25006
• Total number of polymer chains: 3
• Total formula weight: 110734.28

Authors

Li, H.T.,Wang, C.,Chang, T.,Chang, W.C.,Liu, M.Y.,Le Gall, J.,Gui, L.L.,Zhang, J.P.,An, X.M.,Chang, W.R. (deposition date: 2003-12-26, release date: 2004-03-30, Last modification date: 2023-10-25)

Primary citation

Li, H.T.,Wang, C.,Chang, T.,Chang, W.C.,Liu, M.Y.,Le Gall, J.,Gui, L.L.,Zhang, J.P.,An, X.M.,Chang, W.R.
pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes
Biochem.Biophys.Res.Commun., 316:107-113, 2004

PubMed Abstract: Crystal structures of C-terminal despentapeptide nitrite reductase (NiRc-5) from Achromobacter cycloclastes were determined from 1.9 to 2.3A at pH 5.0, 5.4, and 6.2. NiRc-5, that has lost about 30% activity, is found to possess quite similar trimeric structures as the native enzyme. Electron density and copper content measurements indicate that the activity loss is not caused by the release of type 2 copper (T2Cu). pH-profile structural comparisons with native enzyme reveal that the T2Cu active center in NiRc-5 is perturbed, accounting for the partial loss of enzyme activity. This perturbation likely results from the less constrained conformations of two catalytic residues, Asp98 and His255. Hydrogen bonding analysis shows that the deletion of five residues causes a loss of more than half the intersubunit hydrogen bonds mediated by C-terminal tail. This study shows that the C-terminal tail plays an important role in controlling the conformations around the T2Cu site at the subunit interface, and helps keep the optimum microenvironment of active center for the full enzyme activity of AcNiR.

PubMed: 15003518
DOI: 10.1016/j.bbrc.2004.01.177

Experimental method

X-RAY DIFFRACTION (2.2 Å)