Copper nitrite reductase from Sinorhizobium meliloti 2011: Crystal structure and interaction with the physiological versus a nonmetabolically related cupredoxin‐like mediator

2021 ◽  
Author(s):  
Cintia Soledad Ramírez ◽  
Carmien Tolmie ◽  
Diederik Johannes Opperman ◽  
Pablo Javier González ◽  
María Gabriela Rivas ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitrite Reductase ◽  
Sinorhizobium Meliloti

Crystal Structure of the Ligand-Binding Protein EhuB from Sinorhizobium meliloti Reveals Substrate Recognition of the Compatible Solutes Ectoine and Hydroxyectoine

2007 ◽  
Vol 374 (5) ◽  
pp. 1237-1250 ◽  
Author(s):  
Nils Hanekop ◽  
Marina Höing ◽  
Linda Sohn-Bösser ◽  
Mohamed Jebbar ◽  
Lutz Schmitt ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Sinorhizobium Meliloti ◽  
Binding Protein ◽  
Substrate Recognition ◽  
Compatible Solutes

scholarly journals Cytochrome c nitrite reductase from the bacterium Geobacter lovleyi represents a new NrfA subclass

2020 ◽  
Vol 295 (33) ◽  
pp. 11455-11465 ◽  
Author(s):  
Julius Campeciño ◽  
Satyanarayana Lagishetty ◽  
Zdzislaw Wawrzak ◽  
Victor Sosa Alfaro ◽  
Nicolai Lehnert ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitrite Reductase ◽  
Nitrate Reduction ◽  
Convergent Evolution ◽  
Nutrient Loss ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Cytochrome C Nitrite Reductase ◽  
Environmental Bacterium ◽  
Key Driver

Cytochrome c nitrite reductase (NrfA) catalyzes the reduction of nitrite to ammonium in the dissimilatory nitrate reduction to ammonium (DNRA) pathway, a process that competes with denitrification, conserves nitrogen, and minimizes nutrient loss in soils. The environmental bacterium Geobacter lovleyi has recently been recognized as a key driver of DNRA in nature, but its enzymatic pathway is still uncharacterized. To address this limitation, here we overexpressed, purified, and characterized G. lovleyi NrfA. We observed that the enzyme crystallizes as a dimer but remains monomeric in solution. Importantly, its crystal structure at 2.55-Å resolution revealed the presence of an arginine residue in the region otherwise occupied by calcium in canonical NrfA enzymes. The presence of EDTA did not affect the activity of G. lovleyi NrfA, and site-directed mutagenesis of this arginine reduced enzymatic activity to <3% of the WT levels. Phylogenetic analysis revealed four separate emergences of Arg-containing NrfA enzymes. Thus, the Ca2+-independent, Arg-containing NrfA from G. lovleyi represents a new subclass of cytochrome c nitrite reductase. Most genera from the exclusive clades of Arg-containing NrfA proteins are also represented in clades containing Ca2+-dependent enzymes, suggesting convergent evolution.

scholarly journals Crystal structure of C-terminal desundecapeptide nitrite reductase from Achromobacter cycloclastes

2005 ◽  
Vol 338 (4) ◽  
pp. 1935-1942 ◽  
Author(s):  
Hai-Tao Li ◽  
Tschining Chang ◽  
Wen-Chang Chang ◽  
Chung-Jung Chen ◽  
Ming-Yih Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitrite Reductase ◽  
Achromobacter Cycloclastes

scholarly journals Laue crystal structure of Shewanella oneidensis cytochrome c nitrite reductase from a high-yield expression system

2012 ◽  
Vol 17 (4) ◽  
pp. 647-662 ◽  
Author(s):  
Matthew Youngblut ◽  
Evan T. Judd ◽  
Vukica Srajer ◽  
Bilal Sayyed ◽  
Tyler Goelzer ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cytochrome C ◽  
Nitrite Reductase ◽  
Expression System ◽  
Shewanella Oneidensis ◽  
High Yield ◽  
Cytochrome C Nitrite Reductase

Crystal structure of NirD, the small subunit of the nitrite reductase NirbD from Mycobacterium tuberculosis at 2.0 Å resolution

2012 ◽  
Vol 80 (12) ◽  
pp. 2799-2803 ◽  
Author(s):  
Atsushi Izumi ◽  
Robert Schnell ◽  
Gunter Schneider
Keyword(s):  
Crystal Structure ◽  
Mycobacterium Tuberculosis ◽  
Nitrite Reductase ◽  
Small Subunit

scholarly journals pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes

2004 ◽  
Vol 316 (1) ◽  
pp. 107-113 ◽  
Author(s):  
Hai-Tao Li ◽  
Chao Wang ◽  
Tschining Chang ◽  
Wen-Chang Chang ◽  
Ming-Yih Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitrite Reductase ◽  
Ph Profile ◽  
Achromobacter Cycloclastes

The X-ray crystal structure of a pseudoazurin from Sinorhizobium meliloti

2012 ◽  
Vol 115 ◽  
pp. 148-154 ◽  
Author(s):  
Elise M. Laming ◽  
Aaron P. McGrath ◽  
J. Mitchell Guss ◽  
Ulrike Kappler ◽  
Megan J. Maher
Keyword(s):  
Crystal Structure ◽  
Sinorhizobium Meliloti ◽  
X Ray

Crystal structure of a NO-forming nitrite reductase mutant: an analog of a transition state in enzymatic reaction

2003 ◽  
Vol 302 (3) ◽  
pp. 568-574 ◽  
Author(s):  
Sheng-Quan Liu ◽  
Tschining Chang ◽  
Ming-Yih Liu ◽  
Jean LeGall ◽  
Wen-Chang Chang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Transition State ◽  
Nitrite Reductase ◽  
Enzymatic Reaction

Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation

2009 ◽  
Vol 390 (11) ◽  
Author(s):  
Christine Oswald ◽  
Sander H.J. Smits ◽  
Marina Höing ◽  
Erhard Bremer ◽  
Lutz Schmitt
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Ligand Binding ◽  
Closed Form ◽  
Binding Site ◽  
Sinorhizobium Meliloti ◽  
Binding Protein ◽  
Ligand Binding Site ◽  
Abc Transport ◽  
Ligand Free

Abstract The periplasmic ligand-binding protein ChoX is part of the ABC transport system ChoVWX that imports choline as a nutrient into the soil bacterium Sinorhizobium meliloti. We have recently reported the crystal structures of ChoX in complex with its ligands choline and acetylcholine and the structure of a fully closed but substrate-free state of ChoX. This latter structure revealed an architecture of the ligand-binding site that is superimposable to the closed, ligand-bound form of ChoX. We report here the crystal structure of ChoX in an unusual, ligand-free conformation that represents a semi-closed form of ChoX. The analysis revealed a subdomain movement in the N-lobe of ChoX. Comparison with the two well-characterized substrate binding proteins, MBP and HisJ, suggests the presence of a similar subdomain in these proteins.

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