نتایج جستجو برای: metal binding motif

تعداد نتایج: 633452  

Journal: :Applied and environmental microbiology 1998
M Pazirandeh B M Wells R L Ryan

A gene coding for a de novo peptide sequence containing a metal binding motif was chemically synthesized and expressed in Escherichia coli as a fusion with the maltose binding protein. Bacterial cells expressing the metal binding peptide fusion demonstrated enhanced binding of Cd2+ and Hg2+ compared to bacterial cells lacking the metal binding peptide. The potential use of genetically engineere...

Journal: :Biochemical and biophysical research communications 2009
Macarena Marín Dietmar H Pieper

Pseudomonasreinekei MT1 is capable of growing on 4- and 5-chlorosalicylate as the sole carbon source involving a pathway with trans-dienelactone hydrolase as the key enzyme. This enzyme transforms 4-chloromuconolactone to maleylacetate and thereby avoids the spontaneous formation of toxic protoanemonin. trans-Dienelactone hydrolase is a Zn(2+)-dependent hydrolase where activity can be modulated...

2013
Adriana Badarau Arnaud Baslé Susan J. Firbank Christopher Dennison

Although zinc and copper are required by proteins with very different functions, these metals can be delivered to cellular locations by homologous metal transporters within the same organism, as demonstrated by the cyanobacterial ( Synechocystis PCC 6803) zinc exporter ZiaA and thylakoidal copper importer PacS. The N-terminal metal-binding domains of these transporters (ZiaAN and PacSN, respect...

Quorum sensing controls the luminescence of Vibrio fischeri through the transcriptional activator LuxR and the specific autoinducer signal produced by luxI. Amino acid sequences of these two genes were analyzed using bioinformatics tools. LuxI consists of 193 amino acids and appears to contain five α-helices and six ß-sheets when analyzed by SSpro8. LuxI belongs to the autoinducer synthetase fa...

Journal: :Cancer research 1993
R Srinivasan J A Roth S A Maxwell

Mutations within a conserved "conformational" domain of the p53 protein have frequently been observed in a wide variety of human cancers. A hybrid protein containing the wild-type conformational domain of p53 fused to protein A bound to calf thymus DNA and a specific p53 DNA-binding motif. Hybrid proteins containing mutations in p53 bound to DNA less efficiently than wild-type hybrid protein. I...

Journal: :Current opinion in structural biology 2000
A Lewit-Bentley S Réty

The EF-hand motif is the most common calcium-binding motif found in proteins. Several high-resolution structures containing different metal ions bound to EF-hand sites have given new insight into the modulation of their binding affinities. Recently determined structures of members of several newly identified protein families that contain the EF-hand motif in some of their domains, as well as of...

Journal: :Protein science : a publication of the Protein Society 2002
Meng-Jiun Sui Li-Chu Tsai Kuo-Chiang Hsia Lyudmila G Doudeva Wen-Yen Ku Gye Won Han Hanna S Yuan

H-N-H is a motif found in the nuclease domain of a subfamily of bacteria toxins, including colicin E7, that are capable of cleaving DNA nonspecifically. This H-N-H motif has also been identified in a subfamily of homing endonucleases, which cleave DNA site specifically. To better understand the role of metal ions in the H-N-H motif during DNA hydrolysis, we crystallized the nuclease domain of c...

2006
Ramaprasad Srinivasan Jack A. Roth Steve A. Maxwell

Mutations within a conserved "conformational" domain of the p53 protein have frequently been observed in a wide variety of human cancers. A hybrid protein containing the wild-type Conformational domain of p5J fused to protein A bound to calf thymus DNA and a specific p53 DNAbinding motif. Hybrid proteins containing mutations in p53 bound to DNA less efficiently than wild-type hybrid protein. In...

Journal: :Genome research 2002
Fabio Arnesano Lucia Banci Ivano Bertini Simone Ciofi-Baffoni Elena Molteni David L Huffman Thomas V O'Halloran

A comparative structural genomic analysis of a new class of metal-trafficking proteins can provide insights into the intracellular chemistry of reactive cofactors such as copper and zinc. Starting from the sequences of the metallochaperone Atx1 and from the first soluble domain of the copper-transporting ATPase Ccc2, both from yeast, a search on the available genomes was performed using a homol...

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