scholarly journals Metalloregulatory proteins: Metal selectivity and allosteric switching

2011 ◽  
Vol 156 (2-3) ◽  
pp. 103-114 ◽  
Author(s):  
Hermes Reyes-Caballero ◽  
Gregory C. Campanello ◽  
David P. Giedroc
Keyword(s):  
Metal Selectivity ◽  
Metalloregulatory Proteins

scholarly journals Cytosolic Ni(II) Sensor in Cyanobacterium

2012 ◽  
Vol 287 (15) ◽  
pp. 12142-12151 ◽  
Author(s):  
Andrew W. Foster ◽  
Carl J. Patterson ◽  
Rafael Pernil ◽  
Corinna R. Hess ◽  
Nigel J. Robinson
Keyword(s):  
Coordination Sphere ◽  
Promoter Region ◽  
Nitrilotriacetic Acid ◽  
The Other ◽  
Cryptic Promoter ◽  
Difference Spectra ◽  
Inner Membrane ◽  
Fura 2 ◽  
Metal Selectivity ◽  
Metal Sensors

Efflux of surplus Ni(II) across the outer and inner membranes of Synechocystis PCC 6803 is mediated by the Nrs system under the control of a sensor of periplasmic Ni(II), NrsS. Here, we show that the product of ORF sll0176, which encodes a CsoR/RcnR-like protein now designated InrS (for internal nickel-responsive sensor), represses nrsD (NrsD is deduced to efflux Ni(II) across the inner membrane) from a cryptic promoter between the final two ORFs in the nrs operon. Transcripts initiated from the newly identified nrsD promoter accumulate in response to nickel or cobalt but not copper, and recombinant InrS forms specific, Ni(II)-inhibited complexes with the nrsD promoter region. Metal-dependent difference spectra of Ni(II)- and Cu(I)-InrS are similar to Cu(I)-sensing CsoR and dissimilar to Ni(II)/Co(II)-sensing RcnR, consistent with factors beyond the primary coordination sphere switching metal selectivity. Competition with chelators mag-fura-2, nitrilotriacetic acid, EDTA, and EGTA estimate KD Ni(II) for the tightest site of InrS as 2.05 (±1.5) × 10−14m, and weaker KD Ni(II) for the cells' metal sensors of other types: Zn(II) co-repressor Zur, Co(II) activator CoaR, and Zn(II) derepressor ZiaR. Ni(II) transfer to InrS occurs upon addition to Ni(II) forms of each other sensor. InrS binds Ni(II) sufficiently tightly to derepress Ni(II) export at concentrations below KD Ni(II) of the other sensors.

scholarly journals Evolution of Metal Selectivity in Templated Protein Interfaces

2010 ◽  
Vol 132 (25) ◽  
pp. 8610-8617 ◽  
Author(s):  
Jeffrey D. Brodin ◽  
Annette Medina-Morales ◽  
Thomas Ni ◽  
Eric N. Salgado ◽  
Xavier I. Ambroggio ◽  
...  
Keyword(s):  
Protein Interfaces ◽  
Metal Selectivity

Structural and functional studies of SAV1707 from Staphylococcus aureus elucidate its distinct metal-dependent activity and a crucial residue for catalysis

2021 ◽  
Vol 77 (5) ◽  
pp. 587-598
Author(s):  
Dong-Gyun Kim ◽  
Kyu-Yeon Lee ◽  
Sang Jae Lee ◽  
Seung-Ho Cheon ◽  
Yuri Choi ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Metal Binding ◽  
Binding Mode ◽  
Structure And Function ◽  
Functional Study ◽  
Functional Studies ◽  
Dependent Endonuclease ◽  
Metal Selectivity ◽  
Metal Binding Domain ◽  
And Function

The metallo-β-lactamase fold is the most abundant metal-binding domain found in two major kingdoms: bacteria and archaea. Despite the rapid growth in genomic information, most of these enzymes, which may play critical roles in cellular metabolism, remain uncharacterized in terms of structure and function. In this study, X-ray crystal structures of SAV1707, a hypothetical metalloenzyme from Staphylococcus aureus, and its complex with cAMP are reported at high resolutions of 2.05 and 1.55 Å, respectively, with a detailed atomic description. Through a functional study, it was verified that SAV1707 has Ni2+-dependent phosphodiesterase activity and Mn2+-dependent endonuclease activity, revealing a different metal selectivity depending on the reaction. In addition, the crystal structure of cAMP-bound SAV1707 shows a unique snapshot of cAMP that reveals the binding mode of the intermediate, and a key residue Phe511 that forms π–π interactions with cAMP was verified as contributing to substrate recognition by functional studies of its mutant. Overall, these findings characterized the relationship between the structure and function of SAV1707 and may provide further understanding of metalloenzymes possessing the metallo-β-lactamase fold.

scholarly journals Factors governing the competition between group IA and IB cations for monensin A: a DFT/PCM study

RSC Advances ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 5734-5741
Author(s):  
Todor Dudev ◽  
Diana Cheshmedzhieva ◽  
Radoslava Dimitrova ◽  
Peter Dorkov ◽  
Ivayla Pantcheva
Keyword(s):  
Metal Selectivity ◽  
Monensin A

The results obtained suggest that the metal selectivity of monensin can be modulated by changing the solvents used.

Modulating glyoxalase I metal selectivity by deletional mutagenesis: underlying structural factors contributing to nickel activation profiles

Metallomics ◽  
2015 ◽  
Vol 7 (4) ◽  
pp. 605-612 ◽  
Author(s):  
Uthaiwan Suttisansanee ◽  
Yanhong Ran ◽  
Kadia Y. Mullings ◽  
Nicole Sukdeo ◽  
John F. Honek
Keyword(s):  
Protein Engineering ◽  
Glyoxalase I ◽  
Structural Factors ◽  
Metal Selectivity

Switching between the two metal activation classes of glyoxalase I by protein engineering using deletional mutagenesis.

Sign in / Sign up

Export Citation Format

Share Document