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Journal:JBIC:1
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| - | <applet load="Image:JBIC 1.1.pdb" size="500" color="white" frame="true" spin="on" Scene ="Journal:JBIC:1/Jbic1_opening/1" align="right" caption="Crystal structure of cobalt bound adenylate kinase from ''Desulfovibrio gigas''"/> | + | <applet load="Image:JBIC 1.1.pdb" size="500" color="white" frame="true" spin="on" Scene ="Journal:JBIC:1/Jbic1_opening/1" align="right" caption="Crystal structure of cobalt bound adenylate kinase from ''Desulfovibrio gigas'' (<scene name='Journal:JBIC:1/Jbic1_opening/1'>Initial Scene</scene>)"/> |
[[Image: Ak overall metal coord tar.png|350px|left|thumb| Crystal structure of cobalt bound adenylate kinase from ''Desulfovibrio gigas'']] | [[Image: Ak overall metal coord tar.png|350px|left|thumb| Crystal structure of cobalt bound adenylate kinase from ''Desulfovibrio gigas'']] | ||
==Crystal structure of the zinc, cobalt and iron containing adenylate kinase from ''Desulfovibrio gigas'': a novel metal containing adenylate kinase from Gram-negative bacteria== | ==Crystal structure of the zinc, cobalt and iron containing adenylate kinase from ''Desulfovibrio gigas'': a novel metal containing adenylate kinase from Gram-negative bacteria== | ||
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By Dr. Mukhopadhyay & Abhik Mukhopadhyay <br /> | By Dr. Mukhopadhyay & Abhik Mukhopadhyay <br /> | ||
Journal of Biological Inorganic Chemistry - JBIC-10-04-00074.R2 <br /> | Journal of Biological Inorganic Chemistry - JBIC-10-04-00074.R2 <br /> | ||
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The structures of Zn- , Co- and Fe-AK contain the characteristic LID (residues 125-163) and Core (residues 1-124 and 164-223) domains, which also include the AMP binding region. The LID domain harbors the Cys129-X5-His135-X15-Cys151-X2-Cys154- motif, 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 connected to the LID by residues 116-123 and 165-173. This Core domain mainly consists of a five stranded beta sheet surrounded by 5 helices that keep the integrity of the tertiary structure of the enzyme. A Walker motif 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. | The structures of Zn- , Co- and Fe-AK contain the characteristic LID (residues 125-163) and Core (residues 1-124 and 164-223) domains, which also include the AMP binding region. The LID domain harbors the Cys129-X5-His135-X15-Cys151-X2-Cys154- motif, 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 connected to the LID by residues 116-123 and 165-173. This Core domain mainly consists of a five stranded beta sheet surrounded by 5 helices that keep the integrity of the tertiary structure of the enzyme. A Walker motif 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. | ||
| + | <scene name='Journal:JBIC:1/Jbic1_opening/1'>TextToBeDisplayed</scene> | ||
<scene name='Journal:JBIC:1/Cobalt_bound/1'>TextToBeDisplayed</scene> | <scene name='Journal:JBIC:1/Cobalt_bound/1'>TextToBeDisplayed</scene> | ||
Revision as of 15:30, 22 August 2010
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