Sandbox Reserved 1068: Difference between revisions

Line 16:

[[Image:Active_site_cleft.png|300 px|left|thumb|Figure 2: This shows a single sub unit of MbtI, with the active site cleft located at the lower left hand side of the image.]]

The crystal asymmetric unit was found to contain <scene name='69/694235/3log/1'> four MbtI molecules</scene>, however crystal packing and size exclusion chromatography data suggest a monomeric enzyme. There are no significant structural changes between the four monomers excepts from the localized differences in the active site. The overall molecular structure consist of a polypeptide of 450 residues that forms one large single domain with a similar fold to other chromate-utilizing enzymes. The core of the protein is formed by 21 <scene name='69/694235/Beta_sheets/3'>beta-strands</scene> folded into a twisted beta-sandwich. The protein's core is then surrounded by 10 alpha helices(Figure 2).

When the enzyme MbtI preforms its function, it undergoes a conformation change between two major forms. These are the open and closed conformations. The closed conformation presents itself when a loop consisting of residues (323 to 337) partially obstructs the active residues. The open conformation occurs when the loop is not partially obstructing the active resides. The conformation change between the open and closed occurs when the ligand binds, with the open position occurring when a ligand is bound to the enzyme (Harrison).

Sandbox Reserved 1068: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 16: / Line 16: @@
 [[Image:Active_site_cleft.png|300 px|left|thumb|Figure 2: This shows a single sub unit of MbtI, with the active site cleft located at the lower left hand side of the image.]]
 The crystal asymmetric unit was found to contain <scene name='69/694235/3log/1'> four MbtI molecules</scene>, however crystal packing and size exclusion chromatography data suggest a monomeric enzyme. There are no significant structural changes between the four monomers excepts from the localized differences in the active site. The overall molecular structure consist of a polypeptide of 450 residues that forms one large single domain with a similar fold to other chromate-utilizing enzymes. The core of the protein is formed by 21 <scene name='69/694235/Beta_sheets/3'>beta-strands</scene> folded into a twisted beta-sandwich. The protein's core is then surrounded by 10 alpha helices(Figure 2).
-When the enzyme MbtI preforms its function, it undergoes a conformation change between two major forms.  These are the open and closed conformations.  The closed conformation presents itself when a loop consisting of residues (323 to 337) partially obstructs the active residues. The open conformation occurs when the loop is not partially obstructing the active resides.  The conformation change between the open and closed occurs when the ligand binds, with the open position occurring when a ligand is bound to the enzyme (Harrison).