2hjv

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(New page: 200px<br /><applet load="2hjv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hjv, resolution 1.95&Aring;" /> '''Structure of the sec...)
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[[Image:2hjv.gif|left|200px]]<br /><applet load="2hjv" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hjv.gif|left|200px]]<br /><applet load="2hjv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hjv, resolution 1.95&Aring;" />
caption="2hjv, resolution 1.95&Aring;" />
'''Structure of the second domain (residues 207-368) of the Bacillus subtilis YxiN protein'''<br />
'''Structure of the second domain (residues 207-368) of the Bacillus subtilis YxiN protein'''<br />
==Overview==
==Overview==
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The Bacillus subtilis RNA helicase YxiN is a modular three-domain protein., The first two domains form a conserved helicase core that couples an, ATPase activity to an RNA duplex-destabilization activity, while the third, domain recognizes a stem-loop of 23S ribosomal RNA with high affinity and, specificity. The structure of the second domain, amino-acid residues, 207-368, has been solved to 1.95 A resolution, revealing a parallel, alphabeta-fold. The crystallographic asymmetric unit contains two, protomers; superposition shows that they differ substantially in two, segments of peptide that overlap the conserved helicase sequence motifs V, and VI, while the remainder of the domain is isostructural. The, conformational variability of these segments suggests that induced fit is, intrinsic to the recognition of ligands (ATP and RNA) and the coupling of, the ATPase activity to conformational changes.
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The Bacillus subtilis RNA helicase YxiN is a modular three-domain protein. The first two domains form a conserved helicase core that couples an ATPase activity to an RNA duplex-destabilization activity, while the third domain recognizes a stem-loop of 23S ribosomal RNA with high affinity and specificity. The structure of the second domain, amino-acid residues 207-368, has been solved to 1.95 A resolution, revealing a parallel alphabeta-fold. The crystallographic asymmetric unit contains two protomers; superposition shows that they differ substantially in two segments of peptide that overlap the conserved helicase sequence motifs V and VI, while the remainder of the domain is isostructural. The conformational variability of these segments suggests that induced fit is intrinsic to the recognition of ligands (ATP and RNA) and the coupling of the ATPase activity to conformational changes.
==About this Structure==
==About this Structure==
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2HJV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HJV OCA].
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2HJV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJV OCA].
==Reference==
==Reference==
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Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN., Caruthers JM, Hu Y, McKay DB, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1191-5. Epub 2006 Nov 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17142894 17142894]
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Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN., Caruthers JM, Hu Y, McKay DB, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1191-5. Epub 2006 Nov 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17142894 17142894]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Caruthers, J.M.]]
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[[Category: Caruthers, J M.]]
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[[Category: McKay, D.B.]]
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[[Category: McKay, D B.]]
[[Category: parallel alpha-beta]]
[[Category: parallel alpha-beta]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:48:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:40 2008''

Revision as of 15:42, 21 February 2008


2hjv, resolution 1.95Å

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Structure of the second domain (residues 207-368) of the Bacillus subtilis YxiN protein

Overview

The Bacillus subtilis RNA helicase YxiN is a modular three-domain protein. The first two domains form a conserved helicase core that couples an ATPase activity to an RNA duplex-destabilization activity, while the third domain recognizes a stem-loop of 23S ribosomal RNA with high affinity and specificity. The structure of the second domain, amino-acid residues 207-368, has been solved to 1.95 A resolution, revealing a parallel alphabeta-fold. The crystallographic asymmetric unit contains two protomers; superposition shows that they differ substantially in two segments of peptide that overlap the conserved helicase sequence motifs V and VI, while the remainder of the domain is isostructural. The conformational variability of these segments suggests that induced fit is intrinsic to the recognition of ligands (ATP and RNA) and the coupling of the ATPase activity to conformational changes.

About this Structure

2HJV is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN., Caruthers JM, Hu Y, McKay DB, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1191-5. Epub 2006 Nov 30. PMID:17142894

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