Sandbox Reserved 309
From Proteopedia
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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). <ref name=Bellinzoni>PMID: 16672241 </ref> | + | Globular with a central core made by <scene name='Sandbox_Reserved_309/Beta_parallel_sheet/1'>beta parallel sheet</scene> 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> |
=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. <ref name=Bellinzoni>PMID: 16672241 </ref> | 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> | ||
Revision as of 08:58, 31 March 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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| 2cdn, resolution 1.90Å () | |||||||||
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| Ligands: | , | ||||||||
| Activity: | Adenylate kinase, with EC number 2.7.4.3 | ||||||||
| Related: | 1p4s | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
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. [1]
Structure
Protein of 201 residues with a consisting of two molecules of ADP (Adenosine-5'-Phosphate) and Magnesium ion.
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 [2]
The crystalline structure
Globular with a central core made by surrounded by alpha helices, a P-loop motif at the N-terminus that binds ATP, and two regions (LID and NMP). [1]
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. [1]
Catalytic Mechanism
ADP+MgADP↔MgATP+AMP
References
- ↑ 1.0 1.1 1.2 Bellinzoni M, Haouz A, Grana M, Munier-Lehmann H, Shepard W, Alzari PM. The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer. Protein Sci. 2006 Jun;15(6):1489-93. Epub 2006 May 2. PMID:16672241 doi:10.1110/ps.062163406
- ↑ Miron S, Munier-Lehmann H, Craescu CT. Structural and dynamic studies on ligand-free adenylate kinase from Mycobacterium tuberculosis revealed a closed conformation that can be related to the reduced catalytic activity. Biochemistry. 2004 Jan 13;43(1):67-77. PMID:14705932 doi:10.1021/bi0355995
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