Sandbox reserved 392

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<Structure load='1M4D' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin
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<Structure load='1M4D' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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==Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin==
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Anything in this section will appear adjacent to the 3D structure and will be scrollable.
Anything in this section will appear adjacent to the 3D structure and will be scrollable.
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*The Ligands displayed in the molecule to the right are Coenzyme A, 3'-Phosphate-Adenosine-5'-Diphosphate, and Tobramycin. Coenzyme A (CoA) is a coenzyme the synthesizes and oxidizes fatty acids. Tobramycin is an aminoglycoside antibiotic that is used to treat a broad spectrum of bacteria, particularly gram negative. CoA and PAP contain basic and neutral amino acids while Tobramycin consists of acidic and neutral amino acids.
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*The Ligands displayed in the molecule to the right are Coenzyme A, 3'-Phosphate-Adenosine-5'-Diphosphate, and Tobramycin. Coenzyme A (CoA) is a coenzyme that synthesizes and oxidizes fatty acids. Tobramycin is an aminoglycoside antibiotic that is used to treat a broad spectrum of bacteria, particularly gram negative. CoA and PAP contain basic and neutral amino acids while Tobramycin consists of acidic and neutral amino acids.
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*This Shows the possibility that the high affinity aminoglycoside complexes may have the capability to acetylate a key biosynthetic intermediate of mycothiol. Mycothiol is a major reducing agent in the myobacteria. If this occurs it may participate in the regulation of cellular redox potential.
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*"Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin" study researched the possibility that the high affinity aminoglycoside complex may have the capability to acetylate a key biosynthetic intermediate of mycothiol. Mycothiol is a major reducing agent in the myobacteria. If this occurs it may participate in the regulation of cellular redox potential.
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*This molecule represents the secondary structures of the protein. The Alpha helices are represented in pink and the beta strands are represented in yellow. This molecule has approximately 13 alpha helices and approximetly 18 beta strands. Molecule: <scene name='Sandbox_reserved_392/Color_protein_secondarystruct/1'>TextToBeDisplayed</scene>
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*This molecule represents the secondary structures of the protein. The Alpha helices are represented in pink arrows and the beta strands are represented in yellow arrows. This molecule has approximately 13 alpha helices and approximetly 18 beta strands. Molecule: <scene name='Sandbox_reserved_392/Color_protein_secondarystruct/1'>TextToBeDisplayed</scene>
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*This structure focuses on the protein bond to the ligand. The red molecules represent an anionic or negatively charged interaction. The dark blue molecules emphasize the cationic or positively charged interactions. The cationic and anionic interactions are contributed to arginine, aspartic acid, and glycine. The light blue molecules represent Histamine which is a basic amino acid. Molecule: <scene name='Sandbox_reserved_392/Protein-ligand/1'>TextToBeDisplayed</scene>
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*This structure focuses on the protein bond to the ligand. The red molecules represent an anionic or negatively charged interaction. The dark blue molecules emphasize the cationic or positively charged interactions. The cationic and anionic interactions are contributed to arginine, aspartic acid, or glycine amino acids. The light blue molecules represent histidine, which is a basic amino acid. Molecule: <scene name='Sandbox_reserved_392/Protein-ligand/1'>TextToBeDisplayed</scene>
*Reference:
*Reference:

Revision as of 17:58, 18 September 2012

Insert caption here

Drag the structure with the mouse to rotate

Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

  • The Ligands displayed in the molecule to the right are Coenzyme A, 3'-Phosphate-Adenosine-5'-Diphosphate, and Tobramycin. Coenzyme A (CoA) is a coenzyme that synthesizes and oxidizes fatty acids. Tobramycin is an aminoglycoside antibiotic that is used to treat a broad spectrum of bacteria, particularly gram negative. CoA and PAP contain basic and neutral amino acids while Tobramycin consists of acidic and neutral amino acids.
  • "Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin" study researched the possibility that the high affinity aminoglycoside complex may have the capability to acetylate a key biosynthetic intermediate of mycothiol. Mycothiol is a major reducing agent in the myobacteria. If this occurs it may participate in the regulation of cellular redox potential.
  • This molecule represents the secondary structures of the protein. The Alpha helices are represented in pink arrows and the beta strands are represented in yellow arrows. This molecule has approximately 13 alpha helices and approximetly 18 beta strands. Molecule:
  • This structure focuses on the protein bond to the ligand. The red molecules represent an anionic or negatively charged interaction. The dark blue molecules emphasize the cationic or positively charged interactions. The cationic and anionic interactions are contributed to arginine, aspartic acid, or glycine amino acids. The light blue molecules represent histidine, which is a basic amino acid. Molecule:
  • Reference:

<Vetting, M. W., et al. "Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin." RCSB Protien DataBase. N.p., 28 Aug.2002. Web. 13 July 2011. <http://www.rcsb.org/pdb/explore/explore.do?structureId=1M4D>.> Wikipedia. N.p., n.d. Web. 16 Sept. 2012. <http://en.wikipedia.org/wiki/Coenzyme_A>. </StructureSection>

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