User:Andrew Wills/Sandbox 1: Difference between revisions

Line 12:

==Key Structures==

AlkA is composed of three main domains with dimensions of approximately 50 Angstroms, 45 Angstroms, and 25 Angstroms. The first domain (residues 1-112) is the <scene name='56/566536/N-~~terminal~~/1'>N-~~Terminal~~</scene> domain that is composed of a five stranded antiparallel beta sheet and two alpha helices. The <scene name='56/566536/Second_domain/1'>second domain</scene> (residues 113-230) contains seven alpha helices that create a hydrophobic core. The third domain (resudues 231-282) is the <scene name='56/566536/C-terminal/1'>C-Terminal</scene> domain that contains a bundle of three alpha helices (Moe). (Labahn)

AlkA is composed of three main domains with dimensions of approximately 50 Angstroms, 45 Angstroms, and 25 Angstroms. The first domain (residues 1-112) is the <scene name='56/566536/N-terminal_domain/1'>N-terminal</scene> domain that is composed of a five stranded antiparallel beta sheet and two alpha helices. The <scene name='56/566536/Second_domain/1'>second domain</scene> (residues 113-230) contains seven alpha helices that create a hydrophobic core. The third domain (resudues 231-282) is the <scene name='56/566536/C-terminal/1'>C-Terminal</scene> domain that contains a bundle of three alpha helices (Moe). (Labahn)

AlkA is a member of the helix-hairpin-helix (HhH) family of DNA glycosylases, where two compact alpha helical structures are connected by a hairpin loop (Moe). In AlkA, the <scene name='56/566536/Hhh_domain/2'>HhH</scene> domain is composed of residues 202-227 and is responsible for binding the damaged DNA by van der Waals interactions, a few hydrogen bonds, and metal ion interactions.

@@ Line 12: / Line 12: @@
 ==Key Structures==
-AlkA is composed of three main domains with dimensions of approximately 50 Angstroms, 45 Angstroms, and 25 Angstroms. The first domain (residues 1-112) is the <scene name='56/566536/N-terminal/1'>N-Terminal</scene> domain that is composed of a five stranded antiparallel beta sheet and two alpha helices. The <scene name='56/566536/Second_domain/1'>second domain</scene> (residues 113-230) contains seven alpha helices that create a hydrophobic core. The third domain (resudues 231-282) is the <scene name='56/566536/C-terminal/1'>C-Terminal</scene> domain that contains a bundle of three alpha helices (Moe). (Labahn)
+AlkA is composed of three main domains with dimensions of approximately 50 Angstroms, 45 Angstroms, and 25 Angstroms. The first domain (residues 1-112) is the <scene name='56/566536/N-terminal_domain/1'>N-terminal</scene> domain that is composed of a five stranded antiparallel beta sheet and two alpha helices. The <scene name='56/566536/Second_domain/1'>second domain</scene> (residues 113-230) contains seven alpha helices that create a hydrophobic core. The third domain (resudues 231-282) is the <scene name='56/566536/C-terminal/1'>C-Terminal</scene> domain that contains a bundle of three alpha helices (Moe). (Labahn)
 AlkA is a member of the helix-hairpin-helix (HhH) family of DNA glycosylases, where two  compact alpha helical structures are connected by a hairpin loop (Moe).  In AlkA, the <scene name='56/566536/Hhh_domain/2'>HhH</scene> domain is composed of residues 202-227 and is responsible for binding the damaged DNA by van der Waals interactions, a few hydrogen bonds, and metal ion interactions.