The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus
The CsaA protein was first characterized in Bacillus subtilis as a molecular chaperone with export‐related activities. Here we report the 2.0 Å‐resolution crystal structure of the Thermus thermophilus CsaA protein, designated ttCsaA. Atomic structure and experiments in solution revealed a homodimer...
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Published in | The EMBO journal Vol. 20; no. 3; pp. 562 - 569 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Chichester, UK
John Wiley & Sons, Ltd
01.02.2001
Blackwell Publishing Ltd Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | The CsaA protein was first characterized in Bacillus subtilis as a molecular chaperone with export‐related activities. Here we report the 2.0 Å‐resolution crystal structure of the Thermus thermophilus CsaA protein, designated ttCsaA. Atomic structure and experiments in solution revealed a homodimer as the functional unit. The structure of the ttCsaA monomer is reminiscent of the well known oligonucleotide‐binding fold, with the addition of extensions at the N‐ and C‐termini that form an extensive dimer interface. The two identical, large, hydrophobic cavities on the protein surface are likely to constitute the substrate binding sites. The CsaA proteins share essential sequence similarity with the tRNA‐binding protein Trbp111. Structure‐based sequence analysis suggests a close structural resemblance between these proteins, which may extend to the architecture of the binding sites at the atomic level. These results raise the intriguing possibility that CsaA proteins possess a second, tRNA‐binding activity in addition to their export‐related function. |
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Bibliography: | istex:E40297D55134D535CFD6905B005193213CCB0C6B ArticleID:EMBJ7593562 ark:/67375/WNG-G285B3PD-Z ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0261-4189 1460-2075 1460-2075 |
DOI: | 10.1093/emboj/20.3.562 |