Sandbox Reserved 309: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Hezzy Cody (talk | contribs) No edit summary |
Hezzy Cody (talk | contribs) No edit summary |
||
| Line 4: | Line 4: | ||
__TOC__ | __TOC__ | ||
=Introduction/General Information= | =Introduction/General Information= | ||
Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. It is part of the nucleotide and nucleoside kinases family. Its source is the Myobacterium tuberculosis bacterium. Since Adenylate Kinase is found to be essential for bacterial survival, it is targeted by drugs when treating the disease. | Adenylate kinase is a phosphotransferase that catalyzes the interconversion reaction of ATP, ADP, and AMP. It is part of the nucleotide and nucleoside kinases family. Its source is the Myobacterium tuberculosis bacterium. Since Adenylate Kinase is found to be essential for bacterial survival, it is targeted by drugs when treating the disease. <ref name=Bellinzoni>PMID: 16672241 </ref> | ||
=Structure | |||
Protein of 201 residues with a ligand consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion. | =Structure= | ||
< | Protein of 201 residues with a ligand consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion.<scene name='Sandbox_Reserved_309/Ligand/1'>Ligand</scene> | ||
==The solution structure== | ==The solution structure== | ||
With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref> | With no ligand, is represented by a central CORE domain composed of a 5-stranded parallel beta sheet surrounded by 7 alpha helices, and two periferal domains, LID and NMP <ref name=Miron>PMID:14705932 </ref> | ||
==The crystalline structure== | ==The crystalline structure== | ||
Globular with a central core made by beta parallel sheet surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP). | Globular with a central core made by beta parallel sheet surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP). <ref name=Bellinzoni>PMID: 16672241 </ref> | ||
{{STRUCTURE_2cdn|PDB=2cdn|SCENE=}} | {{STRUCTURE_2cdn|PDB=2cdn|SCENE=}} | ||
=Function= | =Function= | ||
Involved in nucleotide biosynthesis. Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP. LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. | Involved in nucleotide biosynthesis. Catalyzes the reversible Mg2+ dependent transfer of the terminal phosphate group from ATP to AMP releasing two molecules of ADP. LID and NMP binding regions go through a significant conformational change during the catalysis reaction depicted below. <ref name=Bellinzoni>PMID: 16672241 </ref> | ||
=Catalytic Mechanism= | =Catalytic Mechanism= | ||
ADP+MgADP↔MgATP+AMP | ADP+MgADP↔MgATP+AMP | ||
*bullet | *bullet | ||
**subbullet | **subbullet | ||
*bullet2 | *bullet2 | ||
<Structure load=2cdn size='200' frame='true' align='left' caption= 'Adenosine-5'-Diphosphate and Mg' scene='Sandbox_Reserved_309/Ligand/1'/> | |||
α | α | ||
=references= | =references= | ||
<references/> | <references/> | ||
