1yt3: Difference between revisions

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[[Image:1yt3.gif|left|200px]]<br /><applet load="1yt3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1yt3.gif|left|200px]]<br /><applet load="1yt3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1yt3, resolution 1.60Å" />

'''Crystal Structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1YT3 OCA].

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==

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[[Category: rnase; exoribonuclease; ribonuclease; exonuclease; nuclease; hydrolase; trna processing]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 07:02:~~15 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:56 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1yt3.gif|left|200px]]<br /><applet load="1yt3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1yt3.gif|left|200px]]<br /><applet load="1yt3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1yt3, resolution 1.60&Aring;" />
 '''Crystal Structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing'''<br />
 ==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.
+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==
-YT3 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YT3 OCA].
+YT3 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==
@@ Line 21: / Line 21: @@
 [[Category: rnase; exoribonuclease; ribonuclease; exonuclease; nuclease; hydrolase; trna processing]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:02:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:56 2008''