Adenylate kinase: Difference between revisions
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[[Adenylate kinase]] (ADK, EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3]) is a phosphotransferase which catalyzes the interconversion of ADP to ATP+AMP. ADK is important in cellular energy homeostasis. Dinucleotides polyphosphates like diadenosine pentaphosphate | [[Adenylate kinase]] (ADK, EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3]) is a phosphotransferase which catalyzes the interconversion of ADP to ATP+AMP. ADK is important in cellular energy homeostasis. Dinucleotides polyphosphates like diadenosine pentaphosphate | ||
(AP5) inhibit ADK. The images at the left and at the right correspond to one representative ADK, ''i.e.'' the crystal structure of Adenylate kinase from ''Desulfovibrio gigas'' ([[3l0p]]). | (AP5) inhibit ADK. The images at the left and at the right correspond to one representative ADK, ''i.e.'' the crystal structure of Adenylate kinase from ''Desulfovibrio gigas'' ([[3l0p]]). | ||
Adenylate kinase is an essential catalyst for cellular growth and multiplication. ADK belongs to a family of enzymes essential to life, and is highly abundant inside the cell. It is involved in the reversible transfer of the terminal phosphate group from Mg2+ATP to Mg2+AMP with high energy turnover: Mg2+ATP + AMP↔Mg2+ADP + ADP. | Adenylate kinase is an essential catalyst for cellular growth and multiplication. ADK belongs to a family of enzymes essential to life, and is highly abundant inside the cell. It is involved in the reversible transfer of the terminal phosphate group from Mg2+ATP to Mg2+AMP with high energy turnover: Mg2+ATP + AMP↔Mg2+ADP + ADP. | ||
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== 3D Structures of Adenylate kinase == | == 3D Structures of Adenylate kinase == | ||
Revision as of 11:21, 14 August 2014
Adenylate kinase (ADK, EC number 2.7.4.3) is a phosphotransferase which catalyzes the interconversion of ADP to ATP+AMP. ADK is important in cellular energy homeostasis. Dinucleotides polyphosphates like diadenosine pentaphosphate (AP5) inhibit ADK. The images at the left and at the right correspond to one representative ADK, i.e. the crystal structure of Adenylate kinase from Desulfovibrio gigas (3l0p). Adenylate kinase is an essential catalyst for cellular growth and multiplication. ADK belongs to a family of enzymes essential to life, and is highly abundant inside the cell. It is involved in the reversible transfer of the terminal phosphate group from Mg2+ATP to Mg2+AMP with high energy turnover: Mg2+ATP + AMP↔Mg2+ADP + ADP.
Adenylate kinases (ADK) from Gram-negative bacteria are generally devoid of metal ions in their LID domain. However, , zinc, cobalt and iron, have been found in ADK from Gram-negative bacteria. Crystal structures of substrate-free ADK from Desulfovibrio gigas with three different metal ions: (2xb4); (3l0s) and (3l0p) bound in its LID domain have been determined by X-ray crystallography. to each other with the same LID domain topology, the only change being the presence of the different metal atoms.
The structures of Zn- , Co- and Fe-ADK contain the and , which also include the AMP binding region. The LID domain harbors the , which is responsible for metal binding in a tetrahedral fashion. In the absence of any substrate, the LID domain of all holo forms of ADK was present in a fully open conformational state. The Core domain is . This Core domain mainly consists of a that keep the integrity of the tertiary structure of the enzyme. A with conserved sequence; G-X-X-G-X-G-K is present in the N-terminal region. The structures presented herein further reinforce the notion that the metal ion is purely structural, contributing to the stability of the LID domain.[1]
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3D Structures of Adenylate kinase3D Structures of Adenylate kinase
Updated on 14-August-2014
ADK unligandedADK unliganded
4ake - EcADK - Escherichia coli
3gmt - ADK - Burkholderia pseudodomallei
3cm0 - ADK - Thermus thermophilus
2rh5 - AaADK - Aquifex aeolicus
1p4s - MtADK - Mycobacterium tuberculosis
2ar7 - hADK 4 - human
3ndp - hADK 4 (mutant)
3iij, 3iik – hADK 6
1ki9 - ADK - Methanococcus thermolithotrophicus
1ak2, 2ak2 - bADK - bovine
3adk - ADK - pig
3be4 - CpADK – Cryptosporidium parvum
3tlx – ADK 2 – Plasmodium falciparum
3umf – ADK – Schistosoma mansoni
4np6 – ADK – Vibrio cholerae
ADK mononucleotide complexADK mononucleotide complex
1ank - EcADK+AMP+AMPPNP
2eck - EcADK+AMP+ADP
3sr0 - AaADK+AMP+ADP + AlF4
2cdn - MtADK+ADP
2bwj - hADK 5+AMP
3iil – hADK 6 + MgADP-Pi
3iim – hADK 6 + DADP
2i6a – hADK + iodotubercidin
2i6b – hADK + acetylinic inhibitor
1kht - ADK+AMP - Methanococcus voltae
1nks - ADK+AMP+ADP - Sulfolobus acidocaldarius
2ak3 - bADK+AMP
1dvr - yADK (mutant)+ATP analog - yeast
ADK complex with dinucletide polyphosphatesADK complex with dinucletide polyphosphates
3hpq, 3hpr, 1e4v, 1e4y - EcADK (mutant)+AP5
1ake - EcADK+AP5
3h86 - ADK+AP5 - Methanococcus maripaludis
3fb4 - ADK+Zn+AP5 - Marinibacillus marinus
3dkv, 3dl0, 1p3j - BsADK+Zn+AP5 - Bacillus subtilis
2qaj, 2oo7, 2p3s, 2ori, 2osb, 2eu8 - BsADK (mutant)+Zn+AP5
2rgx - AaADK+Zn+AP5
3be4 - CpADK+AP5
1z83 – hADK 1+Zn+AP5
2c9y - hADK 2+ A4P
2c95 – hADK 1+ malonate + AP4
2bbw - hADK 4+GP5
1s3g - ADK+Zn+AP5 - Bacillus globisporus
1zak - ADK+AP5 - maize
1zip, 1zin - ADK+Zn+Mn+AP5
1zio – BsADK+Zn+Mg +AP5
1aky, 2aky - yADK+AP5
3aky - yADK (mutant)+AP5
ADK complexes with ionsADK complexes with ions
3l0p - DgADK+Fe - Desulfovibrio gigas
3l0s - DgADK+Co
2xb4 - DgADK+Zn
ReferencesReferences
- ↑ Mukhopadhyay A, Kladova AV, Bursakov SA, Gavel OY, Calvete JJ, Shnyrov VL, Moura I, Moura JJ, Romao MJ, Trincao J. Crystal structure of the zinc-, cobalt-, and iron-containing adenylate kinase from Desulfovibrio gigas: a novel metal-containing adenylate kinase from Gram-negative bacteria. J Biol Inorg Chem. 2010 Sep 7. PMID:20821240 doi:10.1007/s00775-010-0700-8