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1mtp

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{{STRUCTURE_1mtp| PDB=1mtp | SCENE= }}
{{STRUCTURE_1mtp| PDB=1mtp | SCENE= }}
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'''The X-ray crystal structure of a serpin from a thermophilic prokaryote'''
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===The X-ray crystal structure of a serpin from a thermophilic prokaryote===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12679017 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12679017}}
==About this Structure==
==About this Structure==
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[[Category: Protease inhibitor]]
[[Category: Protease inhibitor]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:48:01 2008''

Revision as of 00:48, 29 July 2008

Template:STRUCTURE 1mtp

The X-ray crystal structure of a serpin from a thermophilic prokaryote

Template:ABSTRACT PUBMED 12679017

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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