Journal:JBIC:1
From Proteopedia
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| - | The structures of Zn- , Co- and Fe-AK contain the <scene name='Journal:JBIC:1/Lid_domain/4'>characteristic LID domain (residues 125-163)</scene> and <scene name='Journal:JBIC:1/Core_domain/1'>Core (residues 1-124 and 164-223) domains</scene>, which also include the AMP binding region. The LID domain harbors the <scene name='Journal:JBIC:1/Metal_motif/1'>Cys129-X5-His135-X15-Cys151-X2-Cys154- motif</scene>, which is responsible for metal binding in a tetrahedral fashion. In the absence of any substrate, the LID domain of all holo forms of AK was present in a fully open conformational state. The Core domain is <scene name='Journal:JBIC:1/Core_connection/3'>connected to the LID by residues 116-123 and 165-173</scene>. This Core domain mainly consists of a <scene name='Journal:JBIC:1/Core_helix/3'>five stranded beta sheet surrounded by 5 helices</scene> that keep the integrity of the tertiary structure of the enzyme. A <scene name='Journal:JBIC:1/Walker/ | + | The structures of Zn- , Co- and Fe-AK contain the <scene name='Journal:JBIC:1/Lid_domain/4'>characteristic LID domain (residues 125-163)</scene> and <scene name='Journal:JBIC:1/Core_domain/1'>Core (residues 1-124 and 164-223) domains</scene>, which also include the AMP binding region. The LID domain harbors the <scene name='Journal:JBIC:1/Metal_motif/1'>Cys129-X5-His135-X15-Cys151-X2-Cys154- motif</scene>, which is responsible for metal binding in a tetrahedral fashion. In the absence of any substrate, the LID domain of all holo forms of AK was present in a fully open conformational state. The Core domain is <scene name='Journal:JBIC:1/Core_connection/3'>connected to the LID by residues 116-123 and 165-173</scene>. This Core domain mainly consists of a <scene name='Journal:JBIC:1/Core_helix/3'>five stranded beta sheet surrounded by 5 helices</scene> that keep the integrity of the tertiary structure of the enzyme. A <scene name='Journal:JBIC:1/Walker/3'>Walker motif</scene> with conserved sequence ;<span style="color:#FF0000">G</span>-<span style="color:#FF8040">X</span>-<span style="color:#FFFF00">X</span>-<span style="color:#00FF00">G</span>-<span style="color:#0000FF">X</span>-<span style="color:#FF00FF">G</span>-<span style="color:#00FFFF">K</span> 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. |
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Revision as of 06:02, 24 August 2010
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Crystal structure of the zinc, cobalt and iron containing adenylate kinase from Desulfovibrio gigas: a novel metal containing adenylate kinase from Gram-negative bacteria
A. Mukhopadhyay, A.V. Kladova, O.Yu. Gavel, D.R. Boer, S. Texeira V.L., Shnyrov, Moura, J.J.G. Moura, M.J. Romão, S.A. Bursakov, J. Trincão [1]
Adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3; AK) is an essential catalyst for cellular growth and multiplication. AK 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 (AK) from Gram-negative bacteria are generally devoid of metal ions in their LID domain. However, , zinc, cobalt and iron, have been found in AK from Gram-negative bacteria. Crystal structures of substrate-free AK from Desulfovibrio gigas with three different metal ions ; (; and ) 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-AK 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 AK 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.
- ↑ Mukhopadhyay S, Mukherjee S, Ray BK, Ray A, Stone WL, Das SK. Antioxidant liposomes protect against CEES-induced lung injury by decreasing SAF-1/MAZ-mediated inflammation in the guinea pig lung. J Biochem Mol Toxicol. 2010 May;24(3):187-94. PMID:20583300 doi:10.1002/jbt.20329
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