| + |
GMPPA | form complex 
binding
|
Mannose-1-phosphate guanyltransferase complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281424 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33986552 |
Here, we report the cryo-EM structures of human GMPPA-GMPPB complex, the protein machinery responsible for GDP-Man synthesis, in complex with GDP-Man or GTP. Unexpectedly, we find that the catalytically inactive subunit GMPPA displays a much higher affinity to GDP-Man than the active subunit GMPPB and, subsequently, inhibits the catalytic activity of GMPPB through a unique C-terminal loop of GMPPA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GMPPB | form complex
binding
|
Mannose-1-phosphate guanyltransferase complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281425 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33986552 |
Here, we report the cryo-EM structures of human GMPPA-GMPPB complex, the protein machinery responsible for GDP-Man synthesis, in complex with GDP-Man or GTP. Unexpectedly, we find that the catalytically inactive subunit GMPPA displays a much higher affinity to GDP-Man than the active subunit GMPPB and, subsequently, inhibits the catalytic activity of GMPPB through a unique C-terminal loop of GMPPA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Mannose-1-phosphate guanyltransferase complex | down-regulates quantity 
chemical modification
|
alpha-D-mannose 1-phosphate(2-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281426 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33986552 |
Here, we report the cryo-EM structures of human GMPPA-GMPPB complex, the protein machinery responsible for GDP-Man synthesis, in complex with GDP-Man or GTP. Unexpectedly, we find that the catalytically inactive subunit GMPPA displays a much higher affinity to GDP-Man than the active subunit GMPPB and, subsequently, inhibits the catalytic activity of GMPPB through a unique C-terminal loop of GMPPA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Mannose-1-phosphate guanyltransferase complex | down-regulates quantity
chemical modification
|
GTP(4-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33986552 |
Here, we report the cryo-EM structures of human GMPPA-GMPPB complex, the protein machinery responsible for GDP-Man synthesis, in complex with GDP-Man or GTP. Unexpectedly, we find that the catalytically inactive subunit GMPPA displays a much higher affinity to GDP-Man than the active subunit GMPPB and, subsequently, inhibits the catalytic activity of GMPPB through a unique C-terminal loop of GMPPA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Mannose-1-phosphate guanyltransferase complex | up-regulates quantity 
chemical modification
|
GDP-alpha-D-mannose(2-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281428 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33986552 |
Here, we report the cryo-EM structures of human GMPPA-GMPPB complex, the protein machinery responsible for GDP-Man synthesis, in complex with GDP-Man or GTP. Unexpectedly, we find that the catalytically inactive subunit GMPPA displays a much higher affinity to GDP-Man than the active subunit GMPPB and, subsequently, inhibits the catalytic activity of GMPPB through a unique C-terminal loop of GMPPA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Mannose-1-phosphate guanyltransferase complex