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1sng

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{{STRUCTURE_1sng| PDB=1sng | SCENE= }}
{{STRUCTURE_1sng| PDB=1sng | SCENE= }}
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'''Structure of a Thermophilic Serpin in the Native State'''
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===Structure of a Thermophilic Serpin in the Native State===
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==Overview==
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Serpins fold into a native metastable state and utilize a complex conformational change to inhibit target proteases. An undesirable result of this conformational flexibility is that most inhibitory serpins are heat sensitive, forming inactive polymers at elevated temperatures. However, the prokaryote serpin, thermopin, from Thermobifida fusca is able to function in a heated environment. We have determined the 1.8 A x-ray crystal structure of thermopin in the native, inhibitory conformation. A structural comparison with the previously determined 1.5 A structure of cleaved thermopin provides detailed insight into the complex mechanism of conformational change in serpins. Flexibility in the shutter region and electrostatic interactions at the top of the A beta-sheet (the breach) involving the C-terminal tail, a unique structural feature of thermopin, are postulated to be important for controlling inhibitory activity and triggering conformational change, respectively, in the native state. Here we have discussed the structural basis of how this serpin reconciles the thermodynamic instability necessary for function with the stability required to withstand elevated temperatures.
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The line below this paragraph, {{ABSTRACT_PUBMED_15590653}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15590653 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15590653}}
==About this Structure==
==About this Structure==
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[[Category: Whisstock, J C.]]
[[Category: Whisstock, J C.]]
[[Category: Native state.]]
[[Category: Native state.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:55:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:24:51 2008''

Revision as of 09:24, 28 July 2008

Image:1sng.png

Template:STRUCTURE 1sng

Structure of a Thermophilic Serpin in the Native State

Template:ABSTRACT PUBMED 15590653

About this Structure

1SNG is a Single protein structure of sequence from Thermobifida fusca. Full crystallographic information is available from OCA.

Reference

The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition., Fulton KF, Buckle AM, Cabrita LD, Irving JA, Butcher RE, Smith I, Reeve S, Lesk AM, Bottomley SP, Rossjohn J, Whisstock JC, J Biol Chem. 2005 Mar 4;280(9):8435-42. Epub 2004 Dec 7. PMID:15590653

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