Adenylate kinase: Difference between revisions

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<StructureSection load="" size="350" color=""  spin="on" Scene ="Journal:JBIC:1/Jbic1_opening/2" caption="(PDB code [[3l0p]]) Crystal structure of Fe (orange) bound adenylate kinase complex with glycerol from ''Desulfovibrio gigas''">
<StructureSection load="" size="350" color=""  spin="on" Scene ="Journal:JBIC:1/Jbic1_opening/2" caption="(PDB code [[3l0p]]) Crystal structure of Fe (orange) bound adenylate kinase complex with glycerol from ''Desulfovibrio gigas''">


[[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.  
(AP5) inhibit ADK.  


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&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;Adenylate kinases (ADK) from Gram-negative bacteria are generally devoid of metal ions in their LID domain. However, <scene name='Journal:JBIC:1/Metal_bound/4'>three metal ions</scene>, 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: <scene name='Journal:JBIC:1/Zinc_bound/3'>Zn2+, Zn-ADK</scene> ([[2xb4]]); <scene name='Journal:JBIC:1/Cobalt_bound/7'>Co2+, Co-ADK</scene> ([[3l0s]]) and <scene name='Journal:JBIC:1/Fe_bound/8'>Fe2+, Fe-ADK</scene> ([[3l0p]]) bound in its LID domain have been determined by X-ray crystallography. <scene name='Journal:JBIC:1/Super/10'>All three crystal structures are very similar </scene>to each other with the same LID domain topology, the only change being the presence of the different metal atoms.
&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;Adenylate kinases (ADK) from Gram-negative bacteria are generally devoid of metal ions in their LID domain. However, <scene name='Journal:JBIC:1/Metal_bound/4'>three metal ions</scene>, 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: <scene name='Journal:JBIC:1/Zinc_bound/3'>Zn2+, Zn-ADK</scene> ([[2xb4]]); <scene name='Journal:JBIC:1/Cobalt_bound/7'>Co2+, Co-ADK</scene> ([[3l0s]]) and <scene name='Journal:JBIC:1/Fe_bound/8'>Fe2+, Fe-ADK</scene> ([[3l0p]]) bound in its LID domain have been determined by X-ray crystallography. All three crystal structures are very similar to each other with the same LID domain topology, the only change being the presence of the different metal atoms.
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Alexander Berchansky, Michal Harel