Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2010-06-23

AUTHORS

Asha Manikkoth Balakrishna, Malathy Sony Subramanian Manimekalai, Cornelia Hunke, Shovanlal Gayen, Manfred Rössle, Jeyaraman Jeyakanthan, Gerhard Grüber

ABSTRACT

The structure of the C-terminus of subunit E (E101–206) of Methanocaldococcus jannaschii A-ATP synthase was determined at 4.1 Å. E101–206 consist of a N-terminal globular domain with three α-helices and four antiparallel β-strands and an α-helix at the very C-terminus. Comparison of M. jannaschii E101–206 with the C-terminus E81–198 subunit E from Pyrococcus horikoshii OT3 revealed that the kink in the C-terminal α-helix of E81–198, involved in dimer formation, is absent in M. jannaschii E101–206. Whereas a major dimeric surface interface is present between the P. horikoshii E81–198 molecules in the asymmetric unit, no such interaction could be found in the M. jannaschii E101–206 molecules. To verify the oligomeric behaviour, the low resolution structure of the recombinant E85–206 from M. jannaschii was determined using small angle X-ray scattering. Rigid body modeling of two copies of one of the monomer established a fit with a tail to tail arrangement. More... »

PAGES

311-320

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10863-010-9298-3

DOI

http://dx.doi.org/10.1007/s10863-010-9298-3

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031828402

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20571891


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