1gd7
From Proteopedia
(New page: 200px<br /><applet load="1gd7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gd7, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1gd7.jpg|left|200px]]<br /><applet load="1gd7" size=" | + | [[Image:1gd7.jpg|left|200px]]<br /><applet load="1gd7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gd7, resolution 2.0Å" /> | caption="1gd7, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.'''<br /> | '''CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The CsaA protein was first characterized in Bacillus subtilis as a | + | The CsaA protein was first characterized in Bacillus subtilis as a molecular chaperone with export-related activities. Here we report the 2.0 Angstrom-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. |
==About this Structure== | ==About this Structure== | ||
| - | 1GD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | + | 1GD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GD7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Linde, D.]] | [[Category: Linde, D.]] | ||
[[Category: Muller, J.]] | [[Category: Muller, J.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shibata, T.]] | [[Category: Shibata, T.]] | ||
| - | [[Category: Vassylyev, D | + | [[Category: Vassylyev, D G.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: functional dimer]] | [[Category: functional dimer]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:50 2008'' |
Revision as of 10:48, 21 February 2008
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CRYSTAL STRUCTURE OF A BIFUNCTIONAL PROTEIN (CSAA) WITH EXPORT-RELATED CHAPERONE AND TRNA-BINDING ACTIVITIES.
Overview
The CsaA protein was first characterized in Bacillus subtilis as a molecular chaperone with export-related activities. Here we report the 2.0 Angstrom-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.
About this Structure
1GD7 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus., Kawaguchi S, Muller J, Linde D, Kuramitsu S, Shibata T, Inoue Y, Vassylyev DG, Yokoyama S, EMBO J. 2001 Feb 1;20(3):562-9. PMID:11157762
Page seeded by OCA on Thu Feb 21 12:48:50 2008
Categories: Single protein | Thermus thermophilus | Inoue, Y. | Kawaguchi, S. | Kuramitsu, S. | Linde, D. | Muller, J. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shibata, T. | Vassylyev, D G. | Yokoyama, S. | Functional dimer | Hydrophobic cavity | Oligonucleotide-binding fold | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
