1mtp: Difference between revisions

New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mtp.jpg|left|200px]]<br /><applet load="1mtp" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mtp, resolution 1.5&Aring;" />
caption="1mtp, resolution 1.5&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MTP OCA].  
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.P.]]
[[Category: Bottomley, S P.]]
[[Category: Cabrita, L.D.]]
[[Category: Cabrita, L D.]]
[[Category: Irving, J.A.]]
[[Category: Irving, J A.]]
[[Category: Pike, R.N.]]
[[Category: Pike, R N.]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
[[Category: Whisstock, J.C.]]
[[Category: Whisstock, J C.]]
[[Category: protease inhibitor]]
[[Category: protease inhibitor]]
[[Category: structural genomics]]
[[Category: structural genomics]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:53 2008''

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