Sandbox Reserved 766: Difference between revisions

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== Structure ==

'''Asparagine Synthetase''' is a homodimer comprised of two ~~identical~~ domains ligated together. ASPS consists of a Glutamine Amidotransferase type-2 (residues 2-191) and and Asparagine Synthetase complex (residues 213-536). There are two specific domains that contain the substrate binding sites. The N-terminal domain which contains two layers of anti-parallel beta sheets comprised of six layers each,(site PDB)this is where the Glutamine binds. A C-terminal domain also exists, it is comprised of five parallel beta sheets with alpha helices on either side of it, (site PDB) this is where the Mg2+, ATP and Aspartic Acid bind. The two active sites contained within the terminal domains are linked together by a tunnel of hydrophobic and polar surface amino acid residues.

'''Asparagine Synthetase''' is a homodimer comprised of two domains ligated together. ASPS consists of a Glutamine Amidotransferase type-2 (residues 2-191) and and Asparagine Synthetase complex (residues 213-536). There are two specific domains that contain the substrate binding sites. The N-terminal domain which contains two layers of anti-parallel beta sheets comprised of six layers each,(site PDB)this is where the Glutamine binds. A C-terminal domain also exists, it is comprised of five parallel beta sheets with alpha helices on either side of it, (site PDB) this is where the Mg2+, ATP and Aspartic Acid bind. The two active sites contained within the terminal domains are linked together by a tunnel of hydrophobic and polar surface amino acid residues. Specifically residue 365 is important for the binding of the Beta-Asparty-AMP intermediate into the enzyme.

===Amino Acid Composition===

Sandbox Reserved 766: Difference between revisions

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@@ Line 11: / Line 11: @@
 == Structure ==
-'''Asparagine Synthetase''' is a homodimer comprised of two identical domains ligated together. ASPS consists of a Glutamine Amidotransferase type-2 (residues 2-191) and and Asparagine Synthetase complex (residues 213-536). There are two specific domains that contain the substrate binding sites. The N-terminal domain which contains two layers of anti-parallel beta sheets comprised of six layers each,(site PDB)this is where the Glutamine binds. A C-terminal domain also exists, it is comprised of five parallel beta sheets with alpha helices on either side of it, (site PDB) this is where the Mg2+, ATP and Aspartic Acid bind. The two active sites contained within the terminal domains are linked together by a tunnel of hydrophobic and polar surface amino acid residues.
+'''Asparagine Synthetase''' is a homodimer comprised of two domains ligated together. ASPS consists of a Glutamine Amidotransferase type-2 (residues 2-191) and and Asparagine Synthetase complex (residues 213-536). There are two specific domains that contain the substrate binding sites. The N-terminal domain which contains two layers of anti-parallel beta sheets comprised of six layers each,(site PDB)this is where the Glutamine binds. A C-terminal domain also exists, it is comprised of five parallel beta sheets with alpha helices on either side of it, (site PDB) this is where the Mg2+, ATP and Aspartic Acid bind. The two active sites contained within the terminal domains are linked together by a tunnel of hydrophobic and polar surface amino acid residues. Specifically residue 365 is important for the binding of the Beta-Asparty-AMP intermediate into the enzyme.
 ===Amino Acid Composition===