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Title: Structural proteomics of minimal organisms: conservation ofprotein fold usage and evolutionary implications

Journal Article · · BMC Structural Biology
OSTI ID:895798

Background: Determining the complete repertoire of proteinstructures for all soluble, globular proteins in a single organism hasbeen one of the major goals of several structural genomics projects inrecent years. Results: We report that this goal has nearly been reachedfor several "minimal organisms"--parasites or symbionts with reducedgenomes--for which over 95 percent of the soluble, globular proteins maynow be assigned folds, overall 3-D backbone structures. We analyze thestructures of these proteins as they relate to cellular functions, andcompare conservation off old usage between functional categories. We alsocompare patterns in the conservation off olds among minimal organisms andthose observed between minimal organisms and other bacteria. Conclusion:We find that proteins performing essential cellular functions closelyrelated to transcription and translation exhibit a higher degree ofconservation in fold usage than proteins in other functional categories.Folds related to transcription and translation functional categories werealso over represented in minimal organisms compared to otherbacteria.

Research Organization:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Director, Office of Science; National Institutes ofHealth
DOE Contract Number:
DE-AC02-05CH11231; NIH1-P50-GM62412
OSTI ID:
895798
Report Number(s):
LBNL-59852; R&D Project: 864D2D; BnR: 400412000
Journal Information:
BMC Structural Biology, Vol. 6, Issue 7; Related Information: Journal Publication Date: 03/28/2006
Country of Publication:
United States
Language:
English

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