1n8j
From Proteopedia
(New page: 200px<br /><applet load="1n8j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n8j, resolution 2.17Å" /> '''Crystal Structure of...) |
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| - | [[Image:1n8j.gif|left|200px]]<br /><applet load="1n8j" size=" | + | [[Image:1n8j.gif|left|200px]]<br /><applet load="1n8j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n8j, resolution 2.17Å" /> | caption="1n8j, resolution 2.17Å" /> | ||
'''Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S)'''<br /> | '''Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal | + | Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal transduction. We show that bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction. |
==About this Structure== | ==About this Structure== | ||
| - | 1N8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http:// | + | 1N8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Karplus, P | + | [[Category: Karplus, P A.]] |
| - | [[Category: Poole, L | + | [[Category: Poole, L B.]] |
| - | [[Category: Wood, Z | + | [[Category: Wood, Z A.]] |
[[Category: ahpc]] | [[Category: ahpc]] | ||
[[Category: ahpf]] | [[Category: ahpf]] | ||
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[[Category: peroxiredoxin]] | [[Category: peroxiredoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:23 2008'' |
Revision as of 12:03, 21 February 2008
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Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S)
Overview
Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal transduction. We show that bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction.
About this Structure
1N8J is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling., Wood ZA, Poole LB, Karplus PA, Science. 2003 Apr 25;300(5619):650-3. PMID:12714747
Page seeded by OCA on Thu Feb 21 14:03:23 2008
