1mtp
From Proteopedia
(New page: 200px<br /><applet load="1mtp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mtp, resolution 1.5Å" /> '''The X-ray crystal str...) |
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| - | [[Image:1mtp.jpg|left|200px]]<br /><applet load="1mtp" size=" | + | [[Image:1mtp.jpg|left|200px]]<br /><applet load="1mtp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mtp, resolution 1.5Å" /> | caption="1mtp, resolution 1.5Å" /> | ||
'''The X-ray crystal structure of a serpin from a thermophilic prokaryote'''<br /> | '''The X-ray crystal structure of a serpin from a thermophilic prokaryote'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Serpins utilize conformational change to inhibit target proteinases; the | + | Serpins utilize conformational change to inhibit target proteinases; the price paid for this conformational flexibility is that many undergo temperature-induced polymerization. Despite this thermolability, serpins are present in the genomes of thermophilic prokaryotes, and here we characterize the first such serpin, thermopin. Thermopin is a proteinase inhibitor and, in comparison with human alpha(1)-antitrypsin, possesses enhanced stability at 60 degrees C. The 1.5 A crystal structure reveals novel structural features in regions implicated in serpin folding and stability. Thermopin possesses a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These data provide evidence as to how this unusual serpin has adapted to fold and function in a heated environment. |
==About this Structure== | ==About this Structure== | ||
| - | 1MTP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http:// | + | 1MTP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermobifida fusca]] | [[Category: Thermobifida fusca]] | ||
| - | [[Category: Bottomley, S | + | [[Category: Bottomley, S P.]] |
| - | [[Category: Cabrita, L | + | [[Category: Cabrita, L D.]] |
| - | [[Category: Irving, J | + | [[Category: Irving, J A.]] |
| - | [[Category: Pike, R | + | [[Category: Pike, R N.]] |
[[Category: Rossjohn, J.]] | [[Category: Rossjohn, J.]] | ||
| - | [[Category: Whisstock, J | + | [[Category: Whisstock, J C.]] |
[[Category: protease inhibitor]] | [[Category: protease inhibitor]] | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:53 2008'' |
Revision as of 11:58, 21 February 2008
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The X-ray crystal structure of a serpin from a thermophilic prokaryote
Overview
Serpins utilize conformational change to inhibit target proteinases; the price paid for this conformational flexibility is that many undergo temperature-induced polymerization. Despite this thermolability, serpins are present in the genomes of thermophilic prokaryotes, and here we characterize the first such serpin, thermopin. Thermopin is a proteinase inhibitor and, in comparison with human alpha(1)-antitrypsin, possesses enhanced stability at 60 degrees C. The 1.5 A crystal structure reveals novel structural features in regions implicated in serpin folding and stability. Thermopin possesses a C-terminal "tail" that interacts with the top of the A beta sheet and plays an important role in the folding/unfolding of the molecule. These data provide evidence as to how this unusual serpin has adapted to fold and function in a heated environment.
About this Structure
1MTP is a Protein complex structure of sequences from Thermobifida fusca. Full crystallographic information is available from OCA.
Reference
The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment., Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC, Structure. 2003 Apr;11(4):387-97. PMID:12679017
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