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InterPro: IPR005144 ATP-cone

Protein matchesHelp
UniProtKB
Matches:
3433 proteins
AccessionHelp IPR005144 ATP-cone
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR003796 Ribonucleotide reductase regulator NrdR-like
IPR008926 Ribonucleotide reductase R1 subunit, N-terminal
IPR020872 2-phosphoglycerate kinase
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The ATP-cone is an evolutionarily mobile, ATP-binding regulatory domain which is found in a variety of proteins including ribonucleotide reductases, phosphoglycerate kinases and transcriptional regulators [1].

In ribonucleotide reductase protein R1 (P28903) from Escherichia coli this domain is located at the N terminus, and is composed mostly of helices [2]. It forms part of the allosteric effector region and contains the general allosteric activity site in a cleft located at the tip of the N-terminal region [3]. This site binds either ATP (activating) or dATP (inhibitory), with the base bound in a hydrophobic pocket and the phosphates bound to basic residues. Substrate binding to this site is thought to affect enzyme activity by altering the relative positions of the two subunits of ribonucleotide reductase.

Structural linksHelp
SCOP: a.98.1.1
Database linksHelp
PROSITE doc: PDOC51161
PANDIT: PF03477
Blocks: IPB005144

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005144 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P07742 Ribonucleoside-diphosphate reductase large subunit

P21524 Ribonucleoside-diphosphate reductase large chain 1

P23921 Ribonucleoside-diphosphate reductase large subunit

P48591 Ribonucleoside-diphosphate reductase large subunit

Q03604 Ribonucleoside-diphosphate reductase large subunit

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000788 Ribonucleotide reductase large subunit, C-terminal
IPR008926 Ribonucleotide reductase R1 subunit, N-terminal
IPR013509 Ribonucleotide reductase large subunit, N-terminal
IPR005144 ATP-cone
IPR013346 Ribonucleoside-diphosphate reductase, alpha subunit
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Aravind L, Wolf YI, Koonin EV.
The ATP-cone: an evolutionarily mobile, ATP-binding regulatory domain.
J. Mol. Microbiol. Biotechnol. 2 191-4 2000 [PubMed: 10939243]
2. Uhlin U, Eklund H.
Structure of ribonucleotide reductase protein R1.
Nature 370 533-9 1994 [PubMed: 8052308]
http://dx.doi.org/10.1038/370533a0
3. Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnstrom K, Sjoberg BM, Eklund H.
Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.
Structure 5 1077-92 1997 [PubMed: 9309223]
http://dx.doi.org/10.1016/S0969-2126(97)00259-1

Additional ReadingHelp
Persson AL, Eriksson M, Katterle B, Potsch S, Sahlin M, Sjoberg BM.
A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase.
J. Biol. Chem. 272 1997 31533-41 [PubMed: 9395490]
http://dx.doi.org/10.1074/jbc.272.50.31533
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InterPro 23.1