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8  structures 386  species 0  interactions 439  sequences 7  architectures

Family: ArsD (PF06953)

Summary: Arsenical resistance operon trans-acting repressor ArsD

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This is the Wikipedia entry entitled "Ars operon". More...

Ars operon Edit Wikipedia article

Anion-transporting ATPase
Identifiers
Symbol ArsA_ATPase
Pfam PF02374
Pfam clan CL0023
SCOP 1f48
SUPERFAMILY 1f48
TCDB 3.A.4
ArsB
Identifiers
Symbol ArsB
Pfam PF02040
Pfam clan CL0182
InterPro IPR000802
TCDB 3.A.4
ArsC
PDB 1rw1 EBI.jpg
yffb (pa3664) protein
Identifiers
Symbol ArsC
Pfam PF03960
Pfam clan CL0172
InterPro IPR006660
SCOP 1i9d
SUPERFAMILY 1i9d
ArsD
Identifiers
Symbol ArsD
Pfam PF06953
Pfam clan CL0172
InterPro IPR010712

In molecular biology, the ars operon is an operon found in several bacterial taxon. It is required for the detoxification of arsenate, arsenite, and antimonite.[1] This system transports arsenite and antimonite out of the cell. The pump is composed of two polypeptides, the products of the arsA and arsB genes. This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite before it is extruded. A third gene, arsC, expands the substrate specificity to allow for arsenate pumping and resistance. ArsC is an approximately 150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1 (Grx1). The three ligands must be present simultaneously for reduction to occur.[2]

ArsA and ArsB[edit]

ArsA and ArsB form an anion-translocating ATPase.[3] The ArsB protein is distinguished by its overall hydrophobic character, in keeping with its role as a membrane-associated channel. Sequence analysis reveals the presence of 13 putative transmembrane (TM) regions.

ArsC[edit]

The arsC protein structure has been solved.[4] It belongs to the thioredoxin superfamily fold which is defined by a beta-sheet core surrounded by alpha-helices. The active cysteine residue of ArsC is located in the loop between the first beta-strand and the first helix, which is also conserved in the Spx protein and its homologues.

The arsC family also comprises the Spx proteins which are Gram-positive bacterial transcription factors that regulate the transcription of multiple genes in response to disulphide stress.[5]

ArsD and ArsR[edit]

ArsD is a trans-acting repressor of the arsRDABC operon that confers resistance to arsenicals and antimonials in Escherichia coli. It possesses two-pairs of vicinal cysteine residues, Cys(12)-Cys(13) and Cys(112)-Cys(113), that potentially form separate binding sites for the metalloids that trigger dissociation of ArsD from the operon. However, as a homodimer it has four vicinal cysteine pairs.[6] The ArsD family consists of several bacterial arsenical resistance operon trans-acting repressor ArsD proteins.

ArsR is a trans-acting regulatory protein. It acts as a repressor on the arsRDABC operon when no arsenic is present in the cell. When arsenic is present in the cell ArsR will lose affinity for the operator and RNA polymerase can transcribe the arsDCAB genes.[7][8] ArsD and ArsR work together to regulate the ars operon.[9]

References[edit]

  1. ^ Carlin A, Shi W, Dey S, Rosen BP (February 1995). "The ars operon of Escherichia coli confers arsenical and antimonial resistance". J. Bacteriol. 177 (4): 981–6. PMC 176692. PMID 7860609. 
  2. ^ Liu J, Rosen BP (August 1997). "Ligand interactions of the ArsC arsenate reductase". J. Biol. Chem. 272 (34): 21084–9. doi:10.1074/jbc.272.34.21084. PMID 9261111. 
  3. ^ Rosen BP (1990). "The plasmid-encoded arsenical resistance pump: an anion-translocating ATPase.". Res Microbiol 141 (3): 336–41. PMID 1704144. 
  4. ^ Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF (November 2001). "Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme". Structure 9 (11): 1071–81. doi:10.1016/S0969-2126(01)00672-4. PMID 11709171. 
  5. ^ Zuber P (April 2004). "Spx-RNA polymerase interaction and global transcriptional control during oxidative stress". J. Bacteriol. 186 (7): 1911–8. PMC 374421. PMID 15028674. 
  6. ^ Li S, Rosen BP, Borges-Walmsley MI, Walmsley AR (July 2002). "Evidence for cooperativity between the four binding sites of dimeric ArsD, an As(III)-responsive transcriptional regulator". J. Biol. Chem. 277 (29): 25992–6002. doi:10.1074/jbc.M201619200. PMID 11980902. 
  7. ^ http://www.springerimages.com/Images/RSS/1-10.1007_s00216-009-2785-x-0
  8. ^ http://www.ncbi.nlm.nih.gov/pubmed/9188467?dopt=Abstract
  9. ^ http://www.jbc.org/content/272/22/14257.long

This article incorporates text from the public domain Pfam and InterPro IPR006660

This article incorporates text from the public domain Pfam and InterPro IPR000802

This article incorporates text from the public domain Pfam and InterPro IPR010712

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Arsenical resistance operon trans-acting repressor ArsD Provide feedback

This family consists of several bacterial arsenical resistance operon trans-acting repressor ArsD proteins. ArsD is a trans-acting repressor of the arsRDABC operon that confers resistance to arsenicals and antimonials in Escherichia coli. It possesses two-pairs of vicinal cysteine residues, Cys(12)-Cys(13) and Cys(112)-Cys(113), that potentially form separate binding sites for the metalloids that trigger dissociation of ArsD from the operon. However, as a homodimer it has four vicinal cysteine pairs [1].

Literature references

  1. Li S, Rosen BP, Borges-Walmsley MI, Walmsley AR; , J Biol Chem 2002;277:25992-26002.: Evidence for cooperativity between the four binding sites of dimeric ArsD, an As(III)-responsive transcriptional regulator. PUBMED:11980902 EPMC:11980902


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR010712

This family consists of several bacterial arsenical resistance operon trans-acting repressor ArsD proteins. ArsD is a trans-acting repressor of the arsRDABC operon that confers resistance to arsenicals and antimonials in Escherichia coli. It possesses two-pairs of vicinal cysteine residues, Cys(12)-Cys(13) and Cys(112)-Cys(113), that potentially form separate binding sites for the metalloids that trigger dissociation of ArsD from the operon. However, as a homodimer it has four vicinal cysteine pairs [PUBMED:11980902].

Gene Ontology

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Domain organisation

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Pfam Clan

This family is a member of clan Thioredoxin (CL0172), which has the following description:

This clan contains families related to the thioredoxin family. Thioredoxins are small enzymes that are involved in redox reactions via the reversible oxidation of an active centre disulfide bond. The thioredoxin fold consists of a 3 layer alpha/beta/alpha sandwich and a central beta sheet.

The clan contains the following 45 members:

2Fe-2S_thioredx AhpC-TSA AhpC-TSA_2 ArsC ArsD Calsequestrin DIM1 DSBA DUF1525 DUF1687 DUF2703 DUF4174 DUF836 DUF899 DUF953 ERp29_N Glutaredoxin GSHPx GST_N GST_N_2 GST_N_3 HyaE KaiB MRP-S23 MRP-S25 OST3_OST6 Phosducin Redoxin SCO1-SenC SelP_N SH3BGR T4_deiodinase Thioredox_DsbH Thioredoxin Thioredoxin_2 Thioredoxin_3 Thioredoxin_4 Thioredoxin_5 Thioredoxin_6 Thioredoxin_7 Thioredoxin_8 Thioredoxin_9 Tom37 TraF YtfJ_HI0045

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Full
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Representative proteomes NCBI
(319)
Meta
(11)
RP15
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RP35
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RP55
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RP75
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  Seed
(38)
Full
(439)
Representative proteomes NCBI
(319)
Meta
(11)
RP15
(45)
RP35
(72)
RP55
(86)
RP75
(103)
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Curation and family details

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Seed source: Pfam-B_15383 (release 10.0)
Previous IDs: none
Type: Domain
Author: Moxon SJ
Number in seed: 38
Number in full: 439
Average length of the domain: 115.90 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 90.33 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.7 20.9
Noise cut-off 20.5 20.6
Model length: 123
Family (HMM) version: 6
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Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ArsD domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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