1sng
From Proteopedia
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|PDB= 1sng |SIZE=350|CAPTION= <scene name='initialview01'>1sng</scene>, resolution 1.76Å | |PDB= 1sng |SIZE=350|CAPTION= <scene name='initialview01'>1sng</scene>, resolution 1.76Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=CAF:S-DIMETHYLARSINOYL-CYSTEINE'>CAF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mtp|1mtp]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sng OCA], [http://www.ebi.ac.uk/pdbsum/1sng PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sng RCSB]</span> | ||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: Smith, I.]] | [[Category: Smith, I.]] | ||
[[Category: Whisstock, J C.]] | [[Category: Whisstock, J C.]] | ||
| - | [[Category: SO4]] | ||
[[Category: native state.]] | [[Category: native state.]] | ||
[[Category: serine protease inhibitor (serpin)]] | [[Category: serine protease inhibitor (serpin)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:44:29 2008'' |
Revision as of 20:44, 30 March 2008
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| , resolution 1.76Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1mtp
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a Thermophilic Serpin in the Native State
Overview
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.
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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