2dkf
From Proteopedia
(New page: 200px<br /><applet load="2dkf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2dkf, resolution 2.8Å" /> '''Crystal Structure of ...) |
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==Overview== | ==Overview== | ||
| - | In bacterial RNA metabolism, mRNA degradation is an important process for | + | In bacterial RNA metabolism, mRNA degradation is an important process for gene expression. Recently, a novel ribonuclease (RNase), belonging to the beta-CASP family within the metallo-beta-lactamase superfamily, was identified as a functional homologue of RNase E, a major component for mRNA degradation in Escherichia coli. Here, we have determined the crystal structure of TTHA0252 from Thermus thermophilus HB8, which represents the first report of the tertiary structure of a beta-CASP family protein. TTHA0252 comprises two separate domains: a metallo-beta-lactamase domain and a "clamp" domain. The active site of the enzyme is located in a cleft between the two domains, which includes two zinc ions coordinated by seven conserved residues. Although this configuration is similar to those of other beta-lactamases, TTHA0252 has one conserved His residue characteristic of the beta-CASP family as a ligand. We also detected nuclease activity of TTHA0252 against rRNAs of T. thermophilus. Our results reveal structural and functional aspects of novel RNase E-like enzymes with a beta-CASP fold. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA degradation protein of the metallo-beta-lactamase superfamily., Ishikawa H, Nakagawa N, Kuramitsu S, Masui R, J Biochem | + | Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA degradation protein of the metallo-beta-lactamase superfamily., Ishikawa H, Nakagawa N, Kuramitsu S, Masui R, J Biochem. 2006 Oct;140(4):535-42. Epub 2006 Aug 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16945939 16945939] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: Masui, R.]] | [[Category: Masui, R.]] | ||
[[Category: Nakagawa, N.]] | [[Category: Nakagawa, N.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: thermus thermophilus]] | [[Category: thermus thermophilus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:59:46 2008'' |
Revision as of 14:59, 21 February 2008
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Crystal Structure of TTHA0252 from Thermus thermophilus HB8, a RNA Degradation Protein of the Metallo-beta-lactamase Superfamily
Overview
In bacterial RNA metabolism, mRNA degradation is an important process for gene expression. Recently, a novel ribonuclease (RNase), belonging to the beta-CASP family within the metallo-beta-lactamase superfamily, was identified as a functional homologue of RNase E, a major component for mRNA degradation in Escherichia coli. Here, we have determined the crystal structure of TTHA0252 from Thermus thermophilus HB8, which represents the first report of the tertiary structure of a beta-CASP family protein. TTHA0252 comprises two separate domains: a metallo-beta-lactamase domain and a "clamp" domain. The active site of the enzyme is located in a cleft between the two domains, which includes two zinc ions coordinated by seven conserved residues. Although this configuration is similar to those of other beta-lactamases, TTHA0252 has one conserved His residue characteristic of the beta-CASP family as a ligand. We also detected nuclease activity of TTHA0252 against rRNAs of T. thermophilus. Our results reveal structural and functional aspects of novel RNase E-like enzymes with a beta-CASP fold.
About this Structure
2DKF is a Single protein structure of sequence from Thermus thermophilus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA degradation protein of the metallo-beta-lactamase superfamily., Ishikawa H, Nakagawa N, Kuramitsu S, Masui R, J Biochem. 2006 Oct;140(4):535-42. Epub 2006 Aug 31. PMID:16945939
Page seeded by OCA on Thu Feb 21 16:59:46 2008
Categories: Single protein | Thermus thermophilus | Ishikawa, I. | Kuramitsu, S. | Masui, R. | Nakagawa, N. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | ZN | Beta-casp family | Metallo-beta-lactamase | National project on protein structural and functional analyses | Nppsfa | Ribonuclease | Riken structural genomics/proteomics initiative | Rnase e | Rsgi | Structural genomics
