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Glutamine synthetase is composed of 12 <scene name='Sandbox2qc8/Identical_subunits/1'>identical subunits</scene>. Each subunit is composed of 15 <scene name='Sandbox2qc8/15_alpha_helices/1'>alpha helices</scene> and <scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>15 beta strands</scene>. Each subunit binds 2 Mn for a total of <scene name='Sandbox2qc8/Ligand_mn/1'>24 Mn</scene> per Glutamine Synthetase. | Glutamine synthetase is composed of 12 <scene name='Sandbox2qc8/Identical_subunits/1'>identical subunits</scene>. Each subunit is composed of 15 <scene name='Sandbox2qc8/15_alpha_helices/1'>alpha helices</scene> and <scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>15 beta strands</scene>. Each subunit binds 2 Mn for a total of <scene name='Sandbox2qc8/Ligand_mn/1'>24 Mn</scene> per Glutamine Synthetase. | ||
| - | The beta strands are arranged into 5 <scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>beta sheets</scene>. In addition, there are 5 <scene name='Sandbox2qc8/Hairpins/1'>beta hairpins</scene> and 5 <scene name='Sandbox2qc8/Bulges/1'>beta bulges</scene>. <ref>European Bioinformatics Institute, Ligase(amide synthetase), http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2gls, Accessed December 18, 2008.</ref> β-bulges are distortions in β-sheets resulting from the addition of an extra residue due to mutation. Their presence allows the proteins to conserve their structure by maintaining the hydrogen bond pattern.<ref name="wiley"/>Donald Voet, Judith G. Voet, Charlotte W. Pratt. Fundamentals of Biochemistry life at the molecular level. New Jersey: Wiley,2006.</ref> At the level of the backbone structure, β-bulges can cause a simple aneurysm of the β-sheet. Furthermore, a beta bulge can cause a β-sheet to fold over and cross itself.<br> Within each subunit there are 46 beta turns. These beta turns join secondary structures such as β-sheets and alpha helices when they need to abruptly change directions and usually occur at the protein surface.<ref name="wiley"/> | + | The beta strands are arranged into 5 <scene name='Sandbox2qc8/Pdb_defined_beta_strands/1'>beta sheets</scene>. In addition, there are 5 <scene name='Sandbox2qc8/Hairpins/1'>beta hairpins</scene> and 5 <scene name='Sandbox2qc8/Bulges/1'>beta bulges</scene>. <ref>European Bioinformatics Institute, Ligase(amide synthetase), http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2gls, Accessed December 18, 2008.</ref> β-bulges are distortions in β-sheets resulting from the addition of an extra residue due to mutation. Their presence allows the proteins to conserve their structure by maintaining the hydrogen bond pattern.<ref name="wiley"/>Donald Voet, Judith G. Voet, Charlotte W. Pratt. Fundamentals of Biochemistry life at the molecular level. New Jersey: Wiley,2006.</ref> At the level of the backbone structure, β-bulges can cause a simple aneurysm of the β-sheet. Furthermore, a beta bulge can cause a β-sheet to fold over and cross itself.<br> |
| + | |||
| + | Within each subunit there are 46 beta turns. These beta turns join secondary structures such as β-sheets and alpha helices when they need to abruptly change directions and usually occur at the protein surface.<ref name="wiley"/> | ||
Some important Secondary structures:<br> | Some important Secondary structures:<br> | ||
The <scene name='Sandbox2qc8/12_loops_of_center/1'>beta loops that protrude into the aqueous central channel.</scene> These are important for quaternary stability. <br> | The <scene name='Sandbox2qc8/12_loops_of_center/1'>beta loops that protrude into the aqueous central channel.</scene> These are important for quaternary stability. <br> | ||
Revision as of 03:43, 20 December 2008
Glutamine Synthetase: Secondary structures
Glutamine synthetase is composed of 12 . Each subunit is composed of 15 and . Each subunit binds 2 Mn for a total of per Glutamine Synthetase.
The beta strands are arranged into 5 . In addition, there are 5 and 5 . [1] β-bulges are distortions in β-sheets resulting from the addition of an extra residue due to mutation. Their presence allows the proteins to conserve their structure by maintaining the hydrogen bond pattern.[2]Donald Voet, Judith G. Voet, Charlotte W. Pratt. Fundamentals of Biochemistry life at the molecular level. New Jersey: Wiley,2006.</ref> At the level of the backbone structure, β-bulges can cause a simple aneurysm of the β-sheet. Furthermore, a beta bulge can cause a β-sheet to fold over and cross itself.
Within each subunit there are 46 beta turns. These beta turns join secondary structures such as β-sheets and alpha helices when they need to abruptly change directions and usually occur at the protein surface.[2]
Some important Secondary structures:
The These are important for quaternary stability.
Each subunit has an exposed NH2 terminus and buried COOH terminus as part of a , colored in red. The helical thong is used as an anchor inside another subunit. [3]
The active site within the secondary structure can be called a "bifunnel," providing access to ATP and glutamate at opposing ends.[4]
The only ligand present is a pair of Mn ions (Manganese) that indicates the active site of each subunit of the dodecamer.
Glutamine synthetase contains the .
References
- ↑ European Bioinformatics Institute, Ligase(amide synthetase), http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2gls, Accessed December 18, 2008.
- ↑ Cite error: Invalid
<ref>tag; no text was provided for refs namedwiley - ↑ Yamashita, M., et al.,Refined Atomic Model of Glutamine Synthetase at 3.5A Resolution, The Journal of Biological Chemistry, 1989, 17681-17690.
- ↑ Eisenberg, D., et al., Structure-function relationships of glutamine synthetases, Biochimica et Biophysica Acta 1477 (2000), 122-145.
