Search Results

You searched for all publications:

with publication states 'Published (Approved)'

Search Again...

These results only include publications that have been reviewed and processed by Diamond Light Source. To also view papers that have not yet been processed click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

Exact matches
Related results

2 items found (0 items not approved), displaying all items.1

Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	The polyglutamine expansion at the n-terminal of Huntingtin protein modulates the dynamic configuration and phosphorylation of the c-terminal HEAT domain Taeyang Jung , Baehyun Shin , Giorgio Tamo , Hyeongju Kim , Ravi Vijayvargia , Alexander Leitner , Maria J. Marcaida , Juan Astorga-Wells , Roy Jung , Ruedi Aebersold , Matteo Dal Peraro , Hans Hebert , Ihn Sik Seong , Ji-Joon Song Structure DOI: 10.1016/j.str.2020.06.008 Show Abstract ▼ Abstract: The polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington's disease (HD). The recent cryoelectron microscopy (cryo-EM) structure of HTT-HAP40 complex provided the structural information on its HEAT-repeat domains. Here, we present analyses of the impact of polyQ length on the structure and function of HTT via an integrative structural and biochemical approach. The cryo-EM analysis of normal (Q23) and disease (Q78) type HTTs shows that the structures of apo HTTs significantly differ from the structure of HTT in a HAP40 complex and that the polyQ expansion induces global structural changes in the relative movements among the HTT domains. In addition, we show that the polyQ expansion alters the phosphorylation pattern across HTT and that Ser2116 phosphorylation in turn affects the global structure and function of HTT. These results provide a molecular basis for the effect of the polyQ segment on HTT structure and activity, which may be important for HTT pathology.	Jul 2020
B21-High Throughput SAXS	Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity Gijeong Kim , Liyana Azmi , Seongmin Jang , Taeyang Jung , Hans Hebert , Andrew J. Roe , Olwyn Byron , Ji-Joon Song Nature Communications 10 DOI: 10.1038/s41467-019-12427-8 Diamond Proposal Number(s): [21440] Open Access Show Abstract ▼ Abstract: Aldehyde-alcohol dehydrogenase (AdhE) is a key enzyme in bacterial fermentation, converting acetyl-CoA to ethanol, via two consecutive catalytic reactions. Here, we present a 3.5 Å resolution cryo-EM structure of full-length AdhE revealing a high-order spirosome architecture. The structure shows that the aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) active sites reside at the outer surface and the inner surface of the spirosome respectively, thus topologically separating these two activities. Furthermore, mutations disrupting the helical structure abrogate enzymatic activity, implying that formation of the spirosome structure is critical for AdhE activity. In addition, we show that this spirosome structure undergoes conformational change in the presence of cofactors. This work presents the atomic resolution structure of AdhE and suggests that the high-order helical structure regulates its enzymatic activity.	Oct 2019

Publications Database

Search Results

You searched for all publications:

Search Again...

Subject Areas (check all that apply) select all

Instruments used to collect data (check all that apply) select all

Collaborations involved (check all that apply) select all

Diamond Offline Facilities used

Relevant Technical Areas (check all that apply) select all

Menu for Anonymous User