1qhk

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(New page: 200px<br /><applet load="1qhk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qhk" /> '''N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIA...)
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'''N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9'''<br />
'''N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9'''<br />
==Overview==
==Overview==
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In addition to the conserved and well-defined RNase H domain, eukaryotic, RNases HI possess either one or two copies of a small N-terminal domain., The solution structure of one of the N-terminal domains from Saccharomyces, cerevisiae RNase HI, determined using NMR spectroscopy, is presented. The, 46 residue motif comprises a three-stranded antiparallel beta-sheet and, two short alpha-helices which pack onto opposite faces of the beta-sheet., Conserved residues involved in packing the alpha-helices onto the, beta-sheet form the hydrophobic core of the domain. Three highly conserved, and solvent exposed residues are implicated in RNA binding, W22, K38 and, K39. The beta-beta-alpha-beta-alpha topology of the domain differs from, the structures of known RNA binding domains such as the double-stranded, RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP, motif. However, structural similarities exist between this domain and the, N-terminal domain of ribosomal protein L9 which binds to 23 S ribosomal, RNA.
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In addition to the conserved and well-defined RNase H domain, eukaryotic RNases HI possess either one or two copies of a small N-terminal domain. The solution structure of one of the N-terminal domains from Saccharomyces cerevisiae RNase HI, determined using NMR spectroscopy, is presented. The 46 residue motif comprises a three-stranded antiparallel beta-sheet and two short alpha-helices which pack onto opposite faces of the beta-sheet. Conserved residues involved in packing the alpha-helices onto the beta-sheet form the hydrophobic core of the domain. Three highly conserved and solvent exposed residues are implicated in RNA binding, W22, K38 and K39. The beta-beta-alpha-beta-alpha topology of the domain differs from the structures of known RNA binding domains such as the double-stranded RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP motif. However, structural similarities exist between this domain and the N-terminal domain of ribosomal protein L9 which binds to 23 S ribosomal RNA.
==About this Structure==
==About this Structure==
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1QHK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QHK OCA].
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1QHK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHK OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bycroft, M.]]
[[Category: Bycroft, M.]]
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[[Category: Evans, S.P.]]
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[[Category: Evans, S P.]]
[[Category: ribonuclease hi n-terminal domain]]
[[Category: ribonuclease hi n-terminal domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:42:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:44 2008''

Revision as of 12:39, 21 February 2008


1qhk

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N-TERMINAL DOMAIN OF SACCHAROMYCES CEREVISIAE RNASE HI REVEALS A FOLD WITH A RESEMBLANCE TO THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9

Overview

In addition to the conserved and well-defined RNase H domain, eukaryotic RNases HI possess either one or two copies of a small N-terminal domain. The solution structure of one of the N-terminal domains from Saccharomyces cerevisiae RNase HI, determined using NMR spectroscopy, is presented. The 46 residue motif comprises a three-stranded antiparallel beta-sheet and two short alpha-helices which pack onto opposite faces of the beta-sheet. Conserved residues involved in packing the alpha-helices onto the beta-sheet form the hydrophobic core of the domain. Three highly conserved and solvent exposed residues are implicated in RNA binding, W22, K38 and K39. The beta-beta-alpha-beta-alpha topology of the domain differs from the structures of known RNA binding domains such as the double-stranded RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP motif. However, structural similarities exist between this domain and the N-terminal domain of ribosomal protein L9 which binds to 23 S ribosomal RNA.

About this Structure

1QHK is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Ribonuclease H, with EC number 3.1.26.4 Full crystallographic information is available from OCA.

Reference

NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9., Evans SP, Bycroft M, J Mol Biol. 1999 Aug 20;291(3):661-9. PMID:10448044

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