2.7.6.5: GTP diphosphokinase

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For detailed information about GTP diphosphokinase, go to the full flat file.

Reaction

Synonyms

(p)ppGpp synthase, (p)ppGpp synthetase, (p)ppGpp synthetase I, (p)ppGpp synthetase II, (p)ppGpp synthetase/hydrolase, alarmone synthetase, ATP-GTP 3'-diphosphotransferase, ATP:GTP 3'-pyrophosphotransferase, ATP:GTP pyrophosphoryl transferase, GPSI, GPSII, GTP pyrophosphokinase, guanosine 3',5'-polyphosphate synthase, guanosine 3',5'-polyphosphate synthetase, guanosine 5',3'-polyphosphate synthetase, guanosine pentaphosphate synthetase, ppGpp synthase I, Rel, Rel/Spo protein, RelA, RelMtb, RelMtb protein, RelP, RelSeq, RSH3, SAS 1, SAS 2, SAS1, SF, small alarmone synthase 1, small alarmone synthase 2, small alarmone synthetase 1, stringent factor, YjbM, YwaC

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.6 Diphosphotransferases

                2.7.6.5 GTP diphosphokinase

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Results	in table
17	Activating Compound
15662	AA Sequence
1	Application
1	CAS Registry Number
12	Cloned(Commentary)
4	Cofactor
5	Crystallization (Commentary)
4	Expression
21	General Information
1	General Stability
2	IC50 Value
14	Inhibitors
26	KM Value [mM]
4	Localization
14	Metals/Ions
12	Molecular Weight [Da]
29	Natural Substrates/ Products (Substrates)
98	Organism
5	Pathway
70	PDB ID
2	pH Optimum
1	pI Value
28	Protein Variants
10	Purification (Commentary)
4	Reaction
5	Reaction Type
42	Reference
1	Renatured (Commentary)
14	Source Tissue
6	Specific Activity [micromol/min/mg]
65	Substrates and Products (Substrate)
5	Subunits
76	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
11	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.6.5 - GTP diphosphokinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

nucleotide-free Rel has an elongated conformation in which the TGS domain contacts the synthesis domain by an interface involving alpha-helix 14 and beta strands 7/8 of the synthesis and TGS domains, respectively

Bacillus subtilis

O54408

760841

purified enzyme in presence of ATP and GTP, 1 week, X-ray diffraction structure determination and analysis at 2.94 A resolution

Bacillus subtilis

O31611

739546

cryo-EM structure of RelA in complex with the Escherichia coli 70S ribosome with an average resolution of 3.7 A. RelA adopts an open conformation, where the C-terminal domain is intertwined around an A/T-like tRNA within the intersubunit cavity of the ribosome and the N-terminal domain extends into the solvent

Escherichia coli

P0AG20

762036

structures of RelP in pre-catalytic state (bound to GTP and adenosine 5'-(alpha,beta-methylene)triphosphate), and post-catalytic state (bound to pppGpp). RelP forms a tetramer, but unlike RelQ (SAS1), it is strongly inhibited by both pppGpp and ppGpp and is insensitive to inhibition by RNA. The active site pocket is formed mainly by the beta-strands and the loops beta1/alpha2,alpha3/beta2, and beta3/beta4 in addition to two small helices, alpha2 and alpha5. pppGpp adopts different conformations inside the two active sites (chains A and B) of the dimer

Staphylococcus aureus

W8TMV6

761487

the crystallographic asymmetric unit contains two copies of RelSeq 1-385, two catalytic domains are clearly evident within each monomer, with the hydrolase (residues 5-159) and the synthetase (residues 176-371) domains joined by an overlapping central 3-helix bundle (residues 135-195)

Streptococcus dysgalactiae

-

661439