scholarly journals Engineering the metal-binding loop at a type 1 copper center by circular permutation

RSC Advances ◽  
2017 ◽  
Vol 7 (88) ◽  
pp. 56093-56098
Author(s):  
Honghui Chen ◽  
Binbin Su ◽  
Tongtong Zhang ◽  
Aiping Huang ◽  
Haiping Liu ◽  
...  
Keyword(s):  
Metal Binding ◽  
Circular Permutation ◽  
Type 1 Copper ◽  
Copper Center ◽  
Binding Loop

Circular permutation of the cupredoxin azurin creates a break on the metal binding loop, highlighting the loop's flexibility.

Metal-Binding Loop Length Is a Determinant of the pKaof a Histidine Ligand at a Type 1 Copper Site

2011 ◽  
Vol 50 (2) ◽  
pp. 482-488 ◽  
Author(s):  
Chan Li ◽  
Katsuko Sato ◽  
Stefano Monari ◽  
Isabelle Salard ◽  
Marco Sola ◽  
...  
Keyword(s):  
Metal Binding ◽  
Loop Length ◽  
Copper Site ◽  
Type 1 Copper ◽  
Binding Loop

scholarly journals Effect of circular permutation on the structure and function of type 1 blue copper center in azurin

2016 ◽  
Vol 26 (2) ◽  
pp. 218-226 ◽  
Author(s):  
Yang Yu ◽  
Igor D. Petrik ◽  
Kelly N. Chacón ◽  
Parisa Hosseinzadeh ◽  
Honghui Chen ◽  
...  
Keyword(s):  
Circular Permutation ◽  
Structure And Function ◽  
Blue Copper ◽  
Copper Center ◽  
And Function

scholarly journals A Purple Cupredoxin from Nitrosopumilus maritimus Containing a Mononuclear Type 1 Copper Center with an Open Binding Site

2016 ◽  
Vol 138 (20) ◽  
pp. 6324-6327 ◽  
Author(s):  
Parisa Hosseinzadeh ◽  
Shiliang Tian ◽  
Nicholas M. Marshall ◽  
James Hemp ◽  
Timothy Mullen ◽  
...  
Keyword(s):  
Binding Site ◽  
Type 1 Copper ◽  
Copper Center

The Importance of the Long Type 1 Copper‐Binding Loop of Nitrite Reductase for Structure and Function

2008 ◽  
Vol 14 (19) ◽  
pp. 5820-5828 ◽  
Author(s):  
Katsuko Sato ◽  
Susan J. Firbank ◽  
Chan Li ◽  
Mark J. Banfield ◽  
Christopher Dennison
Keyword(s):  
Nitrite Reductase ◽  
Structure And Function ◽  
Copper Binding ◽  
Type 1 Copper ◽  
And Function ◽  
Binding Loop

Reduction of rhus vernicifera laccase type 1 copper by substituted hydroquinones

1978 ◽  
Vol 8 (3) ◽  
pp. 185-200 ◽  
Author(s):  
Robert A. Holwerda ◽  
John D. Clemmer ◽  
Gerald S. Yoneda ◽  
Billy J. McKerley
Keyword(s):  
Type 1 Copper ◽  
Rhus Vernicifera

An Axial Met Ligand at a Type 1 Copper Site is Preferable for Fast Electron Transfer

ChemBioChem ◽  
2004 ◽  
Vol 5 (11) ◽  
pp. 1579-1581 ◽  
Author(s):  
Mark D. Harrison ◽  
Christopher Dennison
Keyword(s):  
Electron Transfer ◽  
Fast Electron ◽  
Copper Site ◽  
Type 1 Copper

scholarly journals Metal Binding by the D,DX35E Motif of Human Immunodeficiency Virus Type 1 Integrase: Selective Rescue of Cys Substitutions by Mn2+ In Vitro

2004 ◽  
Vol 78 (13) ◽  
pp. 6715-6722 ◽  
Author(s):  
Kui Gao ◽  
Steven Wong ◽  
Frederic Bushman
Keyword(s):  
Metal Binding ◽  
Immunodeficiency Virus ◽  
Acidic Residues ◽  
Metal Cofactor ◽  
Catalytic Role ◽  
Retroviral Integrase ◽  
Metal Cofactors ◽  
Dna Complex

ABSTRACT The D,DX35E motif characteristic of retroviral integrase enzymes (INs) is expected to bind the required metal cofactors (Mg2+ or Mn2+), but direct evidence for a catalytic role has been lacking. Here we used a metal rescue strategy to investigate metal binding. We established conditions for analysis of an activity of IN, disintegration, in both Mg2+ and Mn2+, and tested IN mutants with cysteine substitutions in each acidic residue of the D,DX35E motif. Mn2+ but not Mg2+ can bind tightly to Cys, so if metal binding at the acidic residues is mechanistically important, it is expected that the Cys-substituted enzymes would be active in the presence of Mn2+ only. Of the three acidic residues, a strong metal rescue effect was obtained for D116C, a weaker rescue was seen for D64C, and no rescue was seen with E152C. Modest rescue could also be detected for D116C in normal integration in vitro. Comparison to Ser and Ala substitutions at D116 established that the rescue was selective for Cys. Further studies of the response to pH suggest that the metal cofactor may stabilize the deprotonated nucleophile active in catalysis, and studies of the response to NaCl titrations disclose an additional role for the metal cofactor in stabilizing the IN-DNA complex.

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