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Structural proteomics of minimal organisms: Conservation of protein fold usage and evolutionary implications

✍ Scribed by John-Marc Chandonia; Sung-Hou Kim

Publisher: BioMed Central
Year: 2006
Tongue: English
Weight: 679 KB
Volume: 6
Category: Article
ISSN: 1472-6807
DOI: 10.1186/1472-6807-6-7

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✦ Synopsis

Background

Determining the complete repertoire of protein structures for all soluble, globular proteins in a single organism has been one of the major goals of several structural genomics projects in recent years.

Results

We report that this goal has nearly been reached for several "minimal organisms" – parasites or symbionts with reduced genomes – for which over 95% of the soluble, globular proteins may now be assigned folds, overall 3-D backbone structures. We analyze the structures of these proteins as they relate to cellular functions, and compare conservation of fold usage between functional categories. We also compare patterns in the conservation of folds among minimal organisms and those observed between minimal organisms and other bacteria.

Conclusion

We find that proteins performing essential cellular functions closely related to transcription and translation exhibit a higher degree of conservation in fold usage than proteins in other functional categories. Folds related to transcription and translation functional categories were also overrepresented in minimal organisms compared to other bacteria.

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