Structural Analysis of Proteins in Extreme Saline Environments
Abstract
The objective of the proposed research plan was to elucidate the three-dimensional structure of 2Fe-2S ferredoxin from halobacteria of the Dead Sea and its comparison, to the available structure of a homologous 2Fe-2S ferredoxin from a nonhalophilic source, the algae Spirulina platensis. We wanted to understand what sort of adaptation, on the molecular level, is needed so that a protein can function in a hostile environment such as the Dead Sea. The work carried out during the three years of this project has justified the rationale which served as its basis. Thus the choice of proteins, namely ferredoxin, permitted us to obtain the first three-dimensional structure of a halophilic protein at atomic resolution. This has led to the concept of a solvent domain to help explain the halophilic nature of this protein. Work on the study of the three -dimensional structures of extreme halophilic proteins has continued at the molecular level. During this period we have a) applied a new cryogenic temperature data collection, that we helped to develop, to extend the resolution and improve the quality of our X-ray data for the 2Fe-2S ferredoxin (HmFd) from Halobacterium Marismortui and b) continued our three-dimensional structural studies of the first halophilic enzyme, i.e. malate dehydrogenase (hMDH) also from Halobacterium Marismortui.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 16, 1989
- Accession Number
- ADA212467
Entities
People
- J. L. Sussman
- M. Shoham
Organizations
- Weizmann Institute of Science