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

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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 ... continued below

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Chandonia, John-Marc & Kim, Sung-Hou March 15, 2006.

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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.

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  • Journal Name: BMC Structural Biology; Journal Volume: 6; Journal Issue: 7; Related Information: Journal Publication Date: 03/28/2006

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  • Report No.: LBNL--59852
  • Grant Number: DE-AC02-05CH11231
  • Grant Number: NIH1-P50-GM62412
  • Office of Scientific & Technical Information Report Number: 895798
  • Archival Resource Key: ark:/67531/metadc879601

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  • March 15, 2006

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  • Sept. 22, 2016, 2:13 a.m.

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  • Dec. 15, 2016, 1:32 p.m.

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Chandonia, John-Marc & Kim, Sung-Hou. Structural proteomics of minimal organisms: conservation ofprotein fold usage and evolutionary implications, article, March 15, 2006; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc879601/: accessed December 10, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.