1mtp
From Proteopedia
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| - | [[Image:1mtp.jpg|left|200px]] | + | [[Image:1mtp.jpg|left|200px]] |
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| - | '''The X-ray crystal structure of a serpin from a thermophilic prokaryote''' | + | {{Structure |
| + | |PDB= 1mtp |SIZE=350|CAPTION= <scene name='initialview01'>1mtp</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''The X-ray crystal structure of a serpin from a thermophilic prokaryote''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MTP is a [ | + | 1MTP is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12679017 12679017] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermobifida fusca]] | [[Category: Thermobifida fusca]] | ||
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[[Category: Whisstock, J C.]] | [[Category: Whisstock, J C.]] | ||
[[Category: protease inhibitor]] | [[Category: protease inhibitor]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:48:09 2008'' |
Revision as of 10:48, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 12:48:09 2008
