1wj9
From Proteopedia
(New page: 200px<br /><applet load="1wj9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wj9, resolution 1.90Å" /> '''Crystal structure of...) |
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| - | [[Image:1wj9.jpg|left|200px]]<br /><applet load="1wj9" size=" | + | [[Image:1wj9.jpg|left|200px]]<br /><applet load="1wj9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wj9, resolution 1.90Å" /> | caption="1wj9, resolution 1.90Å" /> | ||
'''Crystal structure of a CRISPR-associated protein from thermus thermophilus'''<br /> | '''Crystal structure of a CRISPR-associated protein from thermus thermophilus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the crystal structure of hypothetical protein TTHB192 | + | We have determined the crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 at 1.9 A resolution. This protein is a member of the Escherichia coli ygcH sequence family, which contains approximately 15 sequence homologs of bacterial origin. These homologs have a high isoelectric point. The crystal structure reveals that TTHB192 consists of two independently folded domains, and that each domain exhibits a ferredoxin-like fold with a four-stranded antiparallel beta-sheet packed on one side by alpha-helices. These two tandem domains face each other to generate a beta-sheet platform. TTHB192 displays overall structural similarity to Sex-lethal protein and poly(A)-binding protein fragments. These proteins have RNA binding activity which is supported by a beta-sheet platform formed by two tandem repeats of an RNA recognition motif domain with signature sequence motifs on the beta-sheet surface. Although TTHB192 does not have the same signature sequence motif as the RNA recognition motif domain, the presence of an evolutionarily conserved basic patch on the beta-sheet platform could be functionally relevant for nucleic acid-binding. This report shows that TTHB192 and its sequence homologs adopt an RNA recognition motif-like domain and provides the first testable functional hypothesis for this protein family. |
==About this Structure== | ==About this Structure== | ||
| - | 1WJ9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | + | 1WJ9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1WJ9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ebihara, A.]] | [[Category: Ebihara, A.]] | ||
[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yao, M.]] | [[Category: Yao, M.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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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 15:45:05 2008'' |
Revision as of 13:45, 21 February 2008
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Crystal structure of a CRISPR-associated protein from thermus thermophilus
Overview
We have determined the crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 at 1.9 A resolution. This protein is a member of the Escherichia coli ygcH sequence family, which contains approximately 15 sequence homologs of bacterial origin. These homologs have a high isoelectric point. The crystal structure reveals that TTHB192 consists of two independently folded domains, and that each domain exhibits a ferredoxin-like fold with a four-stranded antiparallel beta-sheet packed on one side by alpha-helices. These two tandem domains face each other to generate a beta-sheet platform. TTHB192 displays overall structural similarity to Sex-lethal protein and poly(A)-binding protein fragments. These proteins have RNA binding activity which is supported by a beta-sheet platform formed by two tandem repeats of an RNA recognition motif domain with signature sequence motifs on the beta-sheet surface. Although TTHB192 does not have the same signature sequence motif as the RNA recognition motif domain, the presence of an evolutionarily conserved basic patch on the beta-sheet platform could be functionally relevant for nucleic acid-binding. This report shows that TTHB192 and its sequence homologs adopt an RNA recognition motif-like domain and provides the first testable functional hypothesis for this protein family.
About this Structure
1WJ9 is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 reveals a new protein family with an RNA recognition motif-like domain., Ebihara A, Yao M, Masui R, Tanaka I, Yokoyama S, Kuramitsu S, Protein Sci. 2006 Jun;15(6):1494-9. Epub 2006 May 2. PMID:16672237
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