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| | <StructureSection load='2fii' size='340' side='right'caption='[[2fii]], [[Resolution|resolution]] 1.24Å' scene=''> | | <StructureSection load='2fii' size='340' side='right'caption='[[2fii]], [[Resolution|resolution]] 1.24Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fii]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FII FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fii]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FII FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.24Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UAR:URACIL+ARABINOSE-5-PHOSPHATE'>UAR</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UAR:URACIL+ARABINOSE-5-PHOSPHATE'>UAR</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fih|2fih]], [[2fij|2fij]], [[2fil|2fil]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fii OCA], [https://pdbe.org/2fii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fii RCSB], [https://www.ebi.ac.uk/pdbsum/2fii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fii ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fii OCA], [http://pdbe.org/2fii PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fii RCSB], [http://www.ebi.ac.uk/pdbsum/2fii PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fii ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Egli, M]] | + | [[Category: Egli M]] |
| - | [[Category: Li, F]] | + | [[Category: Li F]] |
| - | [[Category: Arabinonucleic acid]]
| + | |
| - | [[Category: B-form dna]]
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| - | [[Category: Dna]]
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| - | [[Category: Sugar modification]]
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| Structural highlights
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li F, Sarkhel S, Wilds CJ, Wawrzak Z, Prakash TP, Manoharan M, Egli M. 2'-Fluoroarabino- and arabinonucleic acid show different conformations, resulting in deviating RNA affinities and processing of their heteroduplexes with RNA by RNase H. Biochemistry. 2006 Apr 4;45(13):4141-52. PMID:16566588 doi:10.1021/bi052322r
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