User talk:Philip C. Sharpe
From Proteopedia
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| - | == | + | ==''' Bio-inorganic Workshop'''== |
<Structure load='1adc' size='500' frame='true' align='right' caption='The contents of this box will change as you click on the the green links below. You can use the mouse to rotate the structure and to zoom in on sections of interest.' scene='Insert optional scene name here' /> | <Structure load='1adc' size='500' frame='true' align='right' caption='The contents of this box will change as you click on the the green links below. You can use the mouse to rotate the structure and to zoom in on sections of interest.' scene='Insert optional scene name here' /> | ||
| - | Read through the instructions on the accompanying worksheet. The | + | Read through the instructions on the accompanying worksheet. The workshop today is about learning how to look at structures of metallo-proteins and understanding how the structure of the metal centre relates to the function of the protein. |
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| - | ==Liver alcohol dehydrogenase, a Zn containing enzyme == | + | =='''Liver alcohol dehydrogenase, a Zn containing enzyme''' == |
| - | <scene name='User_talk:Philip_C._Sharpe/Structural_site_zn_ladh/ | + | The structure on the right is that of liver alcohol dehydrogenase. Clicking on any of the green links below will change the structure displayed in the box. |
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| + | <scene name='User_talk:Philip_C._Sharpe/Structural_site_zn_ladh/3'>Close up of structural Zn site</scene> | ||
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| + | <scene name='User_talk:Philip_C._Sharpe/Catalytic_site_zn_ladh/1'>Close up of catalytic Zn site </scene> | ||
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| + | =='''Urease''' == | ||
| + | Click on the green link below to load the structure of urease. The structure has a pyrophosphate inhibitor bound which has only been partially displayed for the sake of clarity. | ||
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| + | You will also need the link below to a mini-review article by Mazzei, L., Musiani, F. & Ciurli, S. The structure-based reaction mechanism of urease, a nickel dependent enzyme: tale of a long debate. J Biol Inorg Chem 25, 829–845 (2020). https://doi.org/10.1007/s00775-020-01808-w | ||
| + | [https://doi.org/10.1007/s00775-020-01808-w] | ||
| + | <scene name='User_talk:Philip_C._Sharpe/Jack_bean_urease/1'>Jack bean urease</scene> | ||
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| + | <scene name='User_talk:Philip_C._Sharpe/Jack_bean_urease_active_site/1'>Active site of enzyme with bound inhibitor</scene> | ||
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| + | =='''Pseudoazurin''' == | ||
| + | This copper-containing protein acts as an electron transfer protein.The azurin part of the name comes from the intense blue colour of this protein. | ||
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| + | <scene name='User_talk:Philip_C._Sharpe/Pseudoazurin/1'>Pseudoazurin</scene> | ||
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| + | <scene name='User_talk:Philip_C._Sharpe/Pseudoazurin_active_site/1'>Active site of pseudoazurin</scene> | ||
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| + | =='''Assessment Item - Heme proteins''' == | ||
| + | Answer the associated questions on Bb. This is your workshop assessment. In this section, we will look at 3 heme-containing proteins. The three proteins and their functions are described below. Your task is to use the structures, extra information given in the question on Blackboard and your knowledge of transition metal chemistry to match the structures with the correct protein, making sure that you justify your reasoning. '' | ||
| + | |||
| + | {| class="wikitable" | ||
| + | |- | ||
| + | ! Protein !! Function !! Associated reaction | ||
| + | |- | ||
| + | | Catalase || Hydrogen peroxide disproportionation || 2 H<sub>2</sub>O<sub>2</sub> → 2 H<sub>2</sub>O + O<sub>2</sub> | ||
| + | |- | ||
| + | | Cytochrome c (cyt c) || Electron transfer || Fe(II)-cyt c ⇌ Fe(III)-cyt c + e<sup>-</sup> | ||
| + | |- | ||
| + | | Myoglobin (Mb) || Reversible O<sub>2</sub> binding in muscle || Mb + O<sub>2</sub> ⇌ MbO<sub>2</sub> | ||
| + | |} | ||
| + | |||
| + | ===Protein 1=== | ||
| + | <scene name='User_talk:Philip_C._Sharpe/Protein_1/1'>Protein 1</scene> | ||
| + | |||
| + | <scene name='User_talk:Philip_C._Sharpe/Protein_1_active_site/1'>Heme group in Protein 1</scene> | ||
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| + | |||
| + | ===Protein 2=== | ||
| + | <scene name='User_talk:Philip_C._Sharpe/Protein_2/1'>Protein 2</scene> | ||
| + | |||
| + | <scene name='User_talk:Philip_C._Sharpe/Protein_2_heme_group/1'>Heme group in Protein 2</scene> | ||
| + | |||
| + | ===Protein 3=== | ||
| + | <scene name='User_talk:Philip_C._Sharpe/Protein_3/1'>Protein 3, a heme-containing protein</scene> | ||
| + | |||
| + | <scene name='User_talk:Philip_C._Sharpe/Protein_3_heme_group/1'>Heme groups in Protein 3</scene> | ||
Current revision
Contents |
Bio-inorganic Workshop
|
Read through the instructions on the accompanying worksheet. The workshop today is about learning how to look at structures of metallo-proteins and understanding how the structure of the metal centre relates to the function of the protein.
Liver alcohol dehydrogenase, a Zn containing enzyme
The structure on the right is that of liver alcohol dehydrogenase. Clicking on any of the green links below will change the structure displayed in the box.
Urease
Click on the green link below to load the structure of urease. The structure has a pyrophosphate inhibitor bound which has only been partially displayed for the sake of clarity.
You will also need the link below to a mini-review article by Mazzei, L., Musiani, F. & Ciurli, S. The structure-based reaction mechanism of urease, a nickel dependent enzyme: tale of a long debate. J Biol Inorg Chem 25, 829–845 (2020). https://doi.org/10.1007/s00775-020-01808-w
[1]
Pseudoazurin
This copper-containing protein acts as an electron transfer protein.The azurin part of the name comes from the intense blue colour of this protein.
Assessment Item - Heme proteins
Answer the associated questions on Bb. This is your workshop assessment. In this section, we will look at 3 heme-containing proteins. The three proteins and their functions are described below. Your task is to use the structures, extra information given in the question on Blackboard and your knowledge of transition metal chemistry to match the structures with the correct protein, making sure that you justify your reasoning.
| Protein | Function | Associated reaction |
|---|---|---|
| Catalase | Hydrogen peroxide disproportionation | 2 H2O2 → 2 H2O + O2 |
| Cytochrome c (cyt c) | Electron transfer | Fe(II)-cyt c ⇌ Fe(III)-cyt c + e- |
| Myoglobin (Mb) | Reversible O2 binding in muscle | Mb + O2 ⇌ MbO2 |
Protein 1
Protein 2
Protein 3
