scholarly journals Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA

2010 ◽  
pp. n/a-n/a ◽  
Author(s):  
Sorabh Agarwal ◽  
Deli Hong ◽  
Nirav K. Desai ◽  
Matthew H. Sazinsky ◽  
José M. Argüello ◽  
...  
Keyword(s):  
Metal Binding ◽  
Binding Domain ◽  
Archaeoglobus Fulgidus ◽  
Metal Binding Domain

Copper and Zinc Promote Interactions between Membrane-Anchored Peptides of the Metal Binding Domain of the Prion Protein†

Biochemistry ◽  
2007 ◽  
Vol 46 (14) ◽  
pp. 4261-4271 ◽  
Author(s):  
Angela G. Kenward ◽  
Libero J. Bartolotti ◽  
Colin S. Burns
Keyword(s):  
Prion Protein ◽  
Metal Binding ◽  
Binding Domain ◽  
Copper And Zinc ◽  
Metal Binding Domain

Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification

2013 ◽  
Vol 454 (1) ◽  
pp. 147-156 ◽  
Author(s):  
Nataliya V. Dolgova ◽  
Sergiy Nokhrin ◽  
Corey H. Yu ◽  
Graham N. George ◽  
Oleg Y. Dmitriev
Keyword(s):  
Metal Binding ◽  
Wilson’S Disease ◽  
Wilson's Disease ◽  
Binding Domain ◽  
Binding Motif ◽  
Copper Chaperone ◽  
Copper Binding ◽  
Copper Transporters ◽  
Metal Binding Domain ◽  
Disease Protein

Human copper transporters ATP7B (Wilson's disease protein) and ATP7A (Menkes' disease protein) have been implicated in tumour resistance to cisplatin, a widely used anticancer drug. Cisplatin binds to the copper-binding sites in the N-terminal domain of ATP7B, and this binding may be an essential step of cisplatin detoxification involving copper ATPases. In the present study, we demonstrate that cisplatin and a related platinum drug carboplatin produce the same adduct following reaction with MBD2 [metal-binding domain (repeat) 2], where platinum is bound to the side chains of the cysteine residues in the CxxC copper-binding motif. This suggests the same mechanism for detoxification of both drugs by ATP7B. Platinum can also be transferred to MBD2 from copper chaperone Atox1, which was shown previously to bind cisplatin. Binding of the free cisplatin and reaction with the cisplatin-loaded Atox1 produce the same protein-bound platinum intermediate. Transfer of platinum along the copper-transport pathways in the cell may serve as a mechanism of drug delivery to its target in the cell nucleus, and explain tumour-cell resistance to cisplatin associated with the overexpression of copper transporters ATP7B and ATP7A.

The βE-Domain of Wheat Ec-1 Metallothionein: A Metal-Binding Domain with a Distinctive Structure

2009 ◽  
Vol 387 (1) ◽  
pp. 207-218 ◽  
Author(s):  
Estevão A. Peroza ◽  
Roland Schmucki ◽  
Peter Güntert ◽  
Eva Freisinger ◽  
Oliver Zerbe
Keyword(s):  
Metal Binding ◽  
Binding Domain ◽  
Metal Binding Domain ◽  
Distinctive Structure

scholarly journals A possible regulatory role for the metal-binding domain of CadA, the Listeria monocytogenes Cd2+ -ATPase

FEBS Letters ◽  
2001 ◽  
Vol 506 (3) ◽  
pp. 249-252 ◽  
Author(s):  
Nathalie Bal ◽  
Elisabeth Mintz ◽  
Florent Guillain ◽  
Patrice Catty
Keyword(s):  
Listeria Monocytogenes ◽  
Metal Binding ◽  
Binding Domain ◽  
Regulatory Role ◽  
Metal Binding Domain

scholarly journals A Novel Regulatory Metal Binding Domain Is Present in the C Terminus of Arabidopsis Zn2+-ATPase HMA2

2006 ◽  
Vol 281 (45) ◽  
pp. 33881-33891 ◽  
Author(s):  
Elif Eren ◽  
David C. Kennedy ◽  
Michael J. Maroney ◽  
José M. Argüello
Keyword(s):  
Metal Binding ◽  
Binding Domain ◽  
C Terminus ◽  
Metal Binding Domain

scholarly journals A Histidine-rich and Cysteine-rich Metal-binding Domain at the C Terminus of Heat Shock Protein A fromHelicobacter pylori

2008 ◽  
Vol 283 (22) ◽  
pp. 15142-15151 ◽  
Author(s):  
Shujian Cun ◽  
Hongyan Li ◽  
Ruiguang Ge ◽  
Marie C. M. Lin ◽  
Hongzhe Sun
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Metal Binding ◽  
Protein A ◽  
Binding Domain ◽  
C Terminus ◽  
Metal Binding Domain

scholarly journals Hg(II) sequestration and protection by the MerR metal-binding domain (MBD)

Microbiology ◽  
2006 ◽  
Vol 152 (3) ◽  
pp. 709-719 ◽  
Author(s):  
Jie Qin ◽  
Lingyun Song ◽  
Hassan Brim ◽  
Michael J. Daly ◽  
Anne O. Summers
Keyword(s):  
Cell Surface ◽  
Metal Binding ◽  
Deinococcus Radiodurans ◽  
Biochemical Properties ◽  
Binding Domain ◽  
Mercury Resistance ◽  
E Coli ◽  
Metal Binding Domain ◽  
Single Polypeptide ◽  
Physiological And Biochemical

MerR, the metalloregulator of the bacterial mercury resistance (mer) operon, binds Hg(II) with high affinity. To study the mechanism of metal-induced activation, a small protein was previously engineered embodying in a single polypeptide the metal-binding domain (MBD) ordinarily formed between two monomers of MerR. Here the physiological and biochemical properties of MBD expressed on the cell surface or in the cytosol were examined, to better understand the environments in which specific metal binding can occur with this small derivative. Over 20 000 surface copies of MBD were expressed per Escherichia coli cell, with metal stoichiometries of ∼1·0 Hg(II) per MBD monomer. Cells expressing MBD on their surface in rich medium bound 6·1-fold more Hg(II) than those not expressing MBD. Although in nature cells use the entire mer operon to detoxify mercury, it was interesting to note that cells expressing only MBD survived Hg(II) challenge and recovered more quickly than cells without MBD. Cell-surface-expressed MBD bound Hg(II) preferentially even in the presence of a 22-fold molar excess of Zn(II) and when exposed to equimolar Cd(II) in addition. MBD expressed in the cystosol also afforded improved survival from Hg(II) exposure for E. coli and for the completely unrelated bacterium Deinococcus radiodurans.

The N-terminal degenerated metal-binding domain is involved in the heavy metal transport activity of TaHMA2

2015 ◽  
Vol 34 (9) ◽  
pp. 1615-1628 ◽  
Author(s):  
Shuqin Xiang ◽  
Shanshan Feng ◽  
Yuxiu Zhang ◽  
Jinjuan Tan ◽  
Shuang Liang ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Metal Binding ◽  
Metal Transport ◽  
Binding Domain ◽  
Transport Activity ◽  
Metal Binding Domain ◽  
Heavy Metal Transport
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