2fii
From Proteopedia
(New page: 200px<br /><applet load="2fii" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fii, resolution 1.24Å" /> '''Crystal Structure An...) |
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==Overview== | ==Overview== | ||
| - | 2'-Deoxy-2'-fluoro-arabinonucleic acid (FANA) and arabinonucleic acid | + | 2'-Deoxy-2'-fluoro-arabinonucleic acid (FANA) and arabinonucleic acid (ANA) paired to RNA are substrates of RNase H. The conformation of the natural DNA/RNA hybrid substrates appears to be neither A-form nor B-form. Consistent with this, the conformations of FANA and ANA were found to be intermediate between the A- and B-forms. However, FANA opposite RNA is preferred by RNase H over ANA, and the RNA affinity of FANA considerably exceeds that of ANA. By investigating the conformational boundaries of FANA and ANA residues in crystal structures of A- and B-form DNA duplexes at atomic resolution, we demonstrate that FANA and ANA display subtle conformational differences. The structural data provide insight into the structural requirements at the catalytic site of RNase H. They also allow conclusions with regard to the relative importance of stereoelectronic effects and hydration as modulators of RNA affinity. |
==About this Structure== | ==About this Structure== | ||
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[[Category: sugar modifications]] | [[Category: sugar modifications]] | ||
| - | ''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 17:21:42 2008'' |
Revision as of 15:21, 21 February 2008
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Crystal Structure Analysis of the B-DNA Dodecamer CGCGAAT-aU-CGCG, with Incorporated Arabino-Uridin (aU)
Overview
2'-Deoxy-2'-fluoro-arabinonucleic acid (FANA) and arabinonucleic acid (ANA) paired to RNA are substrates of RNase H. The conformation of the natural DNA/RNA hybrid substrates appears to be neither A-form nor B-form. Consistent with this, the conformations of FANA and ANA were found to be intermediate between the A- and B-forms. However, FANA opposite RNA is preferred by RNase H over ANA, and the RNA affinity of FANA considerably exceeds that of ANA. By investigating the conformational boundaries of FANA and ANA residues in crystal structures of A- and B-form DNA duplexes at atomic resolution, we demonstrate that FANA and ANA display subtle conformational differences. The structural data provide insight into the structural requirements at the catalytic site of RNase H. They also allow conclusions with regard to the relative importance of stereoelectronic effects and hydration as modulators of RNA affinity.
About this Structure
2FII is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
2'-Fluoroarabino- and arabinonucleic acid show different conformations, resulting in deviating RNA affinities and processing of their heteroduplexes with RNA by RNase H., Li F, Sarkhel S, Wilds CJ, Wawrzak Z, Prakash TP, Manoharan M, Egli M, Biochemistry. 2006 Apr 4;45(13):4141-52. PMID:16566588
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