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==X- | |||
==X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosine== | |||
<StructureSection load='2cbx' size='340' side='right' caption='[[2cbx]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2cbx' size='340' side='right' caption='[[2cbx]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rqp|1rqp]], [[1rqr|1rqr]], [[2c2w|2c2w]], [[2c4t|2c4t]], [[2c4u|2c4u]], [[2c5b|2c5b]], [[2c5h|2c5h]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rqp|1rqp]], [[1rqr|1rqr]], [[2c2w|2c2w]], [[2c4t|2c4t]], [[2c4u|2c4u]], [[2c5b|2c5b]], [[2c5h|2c5h]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosyl-fluoride_synthase Adenosyl-fluoride synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.63 2.5.1.63] </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=2cbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cbx OCA], [http://pdbe.org/2cbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cbx RCSB], [http://www.ebi.ac.uk/pdbsum/2cbx PDBsum]</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=2cbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cbx OCA], [http://pdbe.org/2cbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cbx RCSB], [http://www.ebi.ac.uk/pdbsum/2cbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cbx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/2cbx_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/2cbx_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 36: | Line 37: | ||
[[Category: Deng, H]] | [[Category: Deng, H]] | ||
[[Category: Hagan, D O]] | [[Category: Hagan, D O]] | ||
[[Category: | [[Category: McEwan, A R]] | ||
[[Category: | [[Category: McGlinchey, R P]] | ||
[[Category: Naismith, J H]] | [[Category: Naismith, J H]] | ||
[[Category: Robinson, D R]] | [[Category: Robinson, D R]] | ||
Revision as of 09:52, 28 March 2018
X-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosineX-ray crystal structure of 5'-fluorodeoxyadenosine synthase from Streptomyces cattleya complexed with beta-D-erythrofuranosyl- adenosine
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C-F bond. We now report that the enzyme will accept 2'-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C-F bond formation. Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates.,Cobb SL, Deng H, McEwan AR, Naismith JH, O'Hagan D, Robinson DA Org Biomol Chem. 2006 Apr 21;4(8):1458-60. Epub 2006 Mar 8. PMID:16604208[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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