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TFQFPFAEQL EKVAEQFPTF QILNEEGEVV NEEAMPELSD EOLKELMRRM : (amino h (amino) (amino i (amino amg (metal) LO apeg 2nd attempt Feedback See Periodic Table O See Hint The structure shown in the viewer was generated from the crystal structure of the heterotetrameric (a2B2) B. stearothermophilus E1 and the peripheral subunit-binding domain from the dihydrolipoyl acetyltransferase (E2) chain of the PDH complex. When you open the viewer, you will see that each subunit in the tetramer is colored differently. First, identify the two Mg2* ions in the structure (one is colored pink, the other blue). This will help you orient to the two active sites within the heterotetramer. Next, use the toolbar along the bottom of the viewer to make the amino acid sequence visible. Find and label the following residues in the structure. (You may wish to make the side chain visible in addition to adding a label.) Glu28, Glu59, Glu88, Asp91, Asp180, Glu183 Complete the sentences below using information from the viewer. These six amino acid residues are split between two subunits. Together, they form a Ohalf acidic an that appears to connect the .Mutation of several of these residues to Ala results in a significant decrease in the decarboxylation activity of the enzyme. Researchers propose that this region may be important for O proton one is catalytically active at a time. between the two active sites to ensure that only

TFQFPFAEQL EKVAEQFPTF QILNEEGEVV NEEAMPELSD EOLKELMRRM : (amino h (amino) (amino i (amino amg (metal) LO apeg 2nd attempt Feedback See Periodic Table O See Hint The structure shown in the viewer was generated from the crystal structure of the heterotetrameric (a2B2) B. stearothermophilus E1 and the peripheral subunit-binding domain from the dihydrolipoyl acetyltransferase (E2) chain of the PDH complex. When you open the viewer, you will see that each subunit in the tetramer is colored differently. First, identify the two Mg2* ions in the structure (one is colored pink, the other blue). This will help you orient to the two active sites within the heterotetramer. Next, use the toolbar along the bottom of the viewer to make the amino acid sequence visible. Find and label the following residues in the structure. (You may wish to make the side chain visible in addition to adding a label.) Glu28, Glu59, Glu88, Asp91, Asp180, Glu183 Complete the sentences below using information from the viewer. These six amino acid residues are split between two subunits. Together, they form a Ohalf acidic an that appears to connect the .Mutation of several of these residues to Ala results in a significant decrease in the decarboxylation activity of the enzyme. Researchers propose that this region may be important for O proton one is catalytically active at a time. between the two active sites to ensure that only

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Complete the sentences below using information from the viewer.

These six amino acid residues are split between two subunits. Together, they form an (acidic/basic) tunnel that appears to connect the two active sites. Mutation of several of these residues to Ala results in a significant decrease in the decarboxylation activity of the enzyme. Researchers propose that this region may be important for  proton shuttling between the two active sites to ensure that only one is catalytically active at a time.

TFQFPFAEQL EKVAEQFPTF QILNEEGEVV NEEAMPELSD EOLKELMRRM : (amino h (amino) (amino i (amino amg (metal) LO apeg 2nd attempt Feedback See Periodic Table O See Hint The structure shown in the viewer was generated from the crystal structure of the heterotetrameric (a2B2) B. stearothermophilus E1 and the peripheral subunit-binding domain from the dihydrolipoyl acetyltransferase (E2) chain of the PDH complex. When you open the viewer, you will see that each subunit in the tetramer is colored differently. First, identify the two Mg2* ions in the structure (one is colored pink, the other blue). This will help you orient to the two active sites within the heterotetramer. Next, use the toolbar along the bottom of the viewer to make the amino acid sequence visible. Find and label the following residues in the structure. (You may wish to make the side chain visible in addition to adding a label.) Glu28, Glu59, Glu88, Asp91, Asp180, Glu183 Complete the sentences below using information from the viewer. These six amino acid residues are split between two subunits. Together, they form a Ohalf acidic an that appears to connect the .Mutation of several of these residues to Ala results in a significant decrease in the decarboxylation activity of the enzyme. Researchers propose that this region may be important for O proton one is catalytically active at a time. between the two active sites to ensure that only
Transcribed Image Text:TFQFPFAEQL EKVAEQFPTF QILNEEGEVV NEEAMPELSD EOLKELMRRM : (amino h (amino) (amino i (amino amg (metal) LO apeg 2nd attempt Feedback See Periodic Table O See Hint The structure shown in the viewer was generated from the crystal structure of the heterotetrameric (a2B2) B. stearothermophilus E1 and the peripheral subunit-binding domain from the dihydrolipoyl acetyltransferase (E2) chain of the PDH complex. When you open the viewer, you will see that each subunit in the tetramer is colored differently. First, identify the two Mg2* ions in the structure (one is colored pink, the other blue). This will help you orient to the two active sites within the heterotetramer. Next, use the toolbar along the bottom of the viewer to make the amino acid sequence visible. Find and label the following residues in the structure. (You may wish to make the side chain visible in addition to adding a label.) Glu28, Glu59, Glu88, Asp91, Asp180, Glu183 Complete the sentences below using information from the viewer. These six amino acid residues are split between two subunits. Together, they form a Ohalf acidic an that appears to connect the .Mutation of several of these residues to Ala results in a significant decrease in the decarboxylation activity of the enzyme. Researchers propose that this region may be important for O proton one is catalytically active at a time. between the two active sites to ensure that only
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