Difference between revisions of "Part:BBa K2710002"
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6xHis Alpha Prefoldin with Spy-Catcher | 6xHis Alpha Prefoldin with Spy-Catcher | ||
| − | ( | + | <p> A HisTag and GSG linker was added to the N-terminus of the protein alpha prefoldin. A SpyCatcher and (GSG)x3 linker was added to the C-terminus. |
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===Usage and Biology=== | ===Usage and Biology=== | ||
<p>Prefoldin is a molecular chaperone protein which assists in the correct folding of nascent proteins<sup>1</sup>. | <p>Prefoldin is a molecular chaperone protein which assists in the correct folding of nascent proteins<sup>1</sup>. | ||
| − | Alpha prefoldin (aPFD) and beta prefoldin (bPFD) are two subclasses of prefoldin which oligomerise to form a heterohexameric structure consisting of two alpha subunits and four beta subunits<sup>1</sup>. Alpha prefoldin (15.7 kDa) and beta prefoldin (13.8 kDa) derived from the thermophilic arcahea <em>Methanobacterium thermoautotrophicum</em> self assemble into an 87 kDa hexamer. The prefoldin hexamer is assembled through interactions between beta hairpins in each subunit, whereby the beta hairpins form two 8 stranded up and down beta barrels<sup>1</sup>. Each subunit contains flexible alpha-helical coiled coils, 60 to 70 Å in length, which extend from the beta barrel platform<sup>1</sup>.</p> | + | Alpha prefoldin (aPFD) and beta prefoldin (bPFD) are two subclasses of prefoldin which oligomerise to form a heterohexameric structure consisting of two alpha subunits and four beta subunits<sup>1</sup>. Alpha prefoldin (15.7 kDa) and beta prefoldin (13.8 kDa) derived from the thermophilic arcahea <em>Methanobacterium thermoautotrophicum</em> self assemble into an 87 kDa hexamer. The prefoldin hexamer is assembled through interactions between beta hairpins in each subunit, whereby the beta hairpins form two 8 stranded up and down beta barrels<sup>1</sup>. Each subunit contains flexible alpha-helical coiled coils, 60 to 70 Å in length, which extend from the beta barrel platform<sup>1</sup>. The hexamer is stable at high temperatures, with a Tm ≥ 70°C<sup>1</sup>.</p> |
| + | <br /> | ||
<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
Revision as of 09:06, 17 October 2018
His-Alpha Prefoldin with SpyCatcher
6xHis Alpha Prefoldin with Spy-Catcher
A HisTag and GSG linker was added to the N-terminus of the protein alpha prefoldin. A SpyCatcher and (GSG)x3 linker was added to the C-terminus.
Usage and Biology
<p>Prefoldin is a molecular chaperone protein which assists in the correct folding of nascent proteins1.
Alpha prefoldin (aPFD) and beta prefoldin (bPFD) are two subclasses of prefoldin which oligomerise to form a heterohexameric structure consisting of two alpha subunits and four beta subunits1. Alpha prefoldin (15.7 kDa) and beta prefoldin (13.8 kDa) derived from the thermophilic arcahea Methanobacterium thermoautotrophicum self assemble into an 87 kDa hexamer. The prefoldin hexamer is assembled through interactions between beta hairpins in each subunit, whereby the beta hairpins form two 8 stranded up and down beta barrels1. Each subunit contains flexible alpha-helical coiled coils, 60 to 70 Å in length, which extend from the beta barrel platform1. The hexamer is stable at high temperatures, with a Tm ≥ 70°C1.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
- Siegert, R., Leroux, M. R., Scheufler, C., Hartl, F. U. & Moarefi, I. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621–32 (2000).
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