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

Abstract

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.

Authors:
;
Publication Date:
Research Org.:
Ernest Orlando Lawrence Berkeley NationalLaboratory, Berkeley, CA (US)
Sponsoring Org.:
USDOE Director, Office of Science; National Institutes ofHealth
OSTI Identifier:
895798
Report Number(s):
LBNL-59852
R&D Project: 864D2D; BnR: 400412000
DOE Contract Number:
DE-AC02-05CH11231; NIH1-P50-GM62412
Resource Type:
Journal Article
Resource Relation:
Journal Name: BMC Structural Biology; Journal Volume: 6; Journal Issue: 7; Related Information: Journal Publication Date: 03/28/2006
Country of Publication:
United States
Language:
English
Subject:
59

Citation Formats

Chandonia, John-Marc, and Kim, Sung-Hou. Structural proteomics of minimal organisms: conservation ofprotein fold usage and evolutionary implications. United States: N. p., 2006. Web.
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Chandonia, John-Marc, & Kim, Sung-Hou. Structural proteomics of minimal organisms: conservation ofprotein fold usage and evolutionary implications. United States.
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Chandonia, John-Marc, and Kim, Sung-Hou. Wed . "Structural proteomics of minimal organisms: conservation ofprotein fold usage and evolutionary implications". United States. doi:. https://www.osti.gov/servlets/purl/895798.
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@article{osti_895798,
title = {Structural proteomics of minimal organisms: conservation ofprotein fold usage and evolutionary implications},
author = {Chandonia, John-Marc and Kim, Sung-Hou},
abstractNote = {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.},
doi = {},
journal = {BMC Structural Biology},
number = 7,
volume = 6,
place = {United States},
year = {Wed Mar 15 00:00:00 EST 2006},
month = {Wed Mar 15 00:00:00 EST 2006}
}
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