1yt3
From Proteopedia
(New page: 200px<br /><applet load="1yt3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yt3, resolution 1.60Å" /> '''Crystal Structure of...) |
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| - | [[Image:1yt3.gif|left|200px]]<br /><applet load="1yt3" size=" | + | [[Image:1yt3.gif|left|200px]]<br /><applet load="1yt3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yt3, resolution 1.60Å" /> | caption="1yt3, resolution 1.60Å" /> | ||
'''Crystal Structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing'''<br /> | '''Crystal Structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing'''<br /> | ||
==Overview== | ==Overview== | ||
| - | RNase D (RND) is one of seven exoribonucleases identified in Escherichia | + | RNase D (RND) is one of seven exoribonucleases identified in Escherichia coli. RNase D has homologs in many eubacteria and eukaryotes, and has been shown to contribute to the 3' maturation of several stable RNAs. Here, we report the 1.6 A resolution crystal structure of E. coli RNase D. The conserved DEDD residues of RNase D fold into an arrangement very similar to the Klenow fragment exonuclease domain. Besides the catalytic domain, RNase D also contains two structurally similar alpha-helical domains with no discernible sequence homology between them. These closely resemble the HRDC domain previously seen in RecQ-family helicases and several other proteins acting on nucleic acids. More interestingly, the DEDD catalytic domain and the two helical domains come together to form a ring-shaped structure. The ring-shaped architecture of E. coli RNase D and the HRDC domains likely play a major role in determining the substrate specificity of this exoribonuclease. |
==About this Structure== | ==About this Structure== | ||
| - | 1YT3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_III Ribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.3 3.1.26.3] Full crystallographic information is available from [http:// | + | 1YT3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_III Ribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.3 3.1.26.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YT3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rnase; exoribonuclease; ribonuclease; exonuclease; nuclease; hydrolase; trna processing]] | [[Category: rnase; exoribonuclease; ribonuclease; exonuclease; nuclease; hydrolase; trna processing]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:56 2008'' |
Revision as of 14:08, 21 February 2008
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Crystal Structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing
Overview
RNase D (RND) is one of seven exoribonucleases identified in Escherichia coli. RNase D has homologs in many eubacteria and eukaryotes, and has been shown to contribute to the 3' maturation of several stable RNAs. Here, we report the 1.6 A resolution crystal structure of E. coli RNase D. The conserved DEDD residues of RNase D fold into an arrangement very similar to the Klenow fragment exonuclease domain. Besides the catalytic domain, RNase D also contains two structurally similar alpha-helical domains with no discernible sequence homology between them. These closely resemble the HRDC domain previously seen in RecQ-family helicases and several other proteins acting on nucleic acids. More interestingly, the DEDD catalytic domain and the two helical domains come together to form a ring-shaped structure. The ring-shaped architecture of E. coli RNase D and the HRDC domains likely play a major role in determining the substrate specificity of this exoribonuclease.
About this Structure
1YT3 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Ribonuclease III, with EC number 3.1.26.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing., Zuo Y, Wang Y, Malhotra A, Structure. 2005 Jul;13(7):973-84. PMID:16004870
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