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4bwv
From Proteopedia
(Difference between revisions)
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| - | + | ==Structure of Adenosine 5-prime-phosphosulfate Reductase apr-b from Physcomitrella Patens== | |
| - | + | <StructureSection load='4bwv' size='340' side='right' caption='[[4bwv]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4bwv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Moss Moss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BWV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_reductase_(thioredoxin) Adenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.10 1.8.4.10] </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=4bwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bwv RCSB], [http://www.ebi.ac.uk/pdbsum/4bwv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sulfonucleotide reductases catalyse the first reductive step of sulfate assimilation. Their substrate specificities generally correlate with the requirement for a [Fe4S4] cluster, where adenosine 5'-phosphosulfate (APS) reductases possess a cluster and 3'-phosphoadenosine 5'-phosphosulfate reductases do not. The exception is the APR-B isoform of APS reductase from the moss Physcomitrella patens, which lacks a cluster. The crystal structure of APR-B, the first for a plant sulfonucleotide reductase, is consistent with a preference for APS. Structural conservation with bacterial APS reductase rules out a structural role for the cluster, but supports the contention that it enhances the activity of conventional APS reductases. | ||
| - | + | The X-ray crystal structure of APR-B, an atypical adenosine 5'-phosphosulfate reductase from Physcomitrella patens.,Stevenson CE, Hughes RK, McManus MT, Lawson DM, Kopriva S FEBS Lett. 2013 Nov 15;587(22):3626-32. doi: 10.1016/j.febslet.2013.09.034. Epub , 2013 Oct 4. PMID:24100135<ref>PMID:24100135</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Hughes, R K | + | == References == |
| - | [[Category: Kopriva, S | + | <references/> |
| - | [[Category: Lawson, D M | + | __TOC__ |
| - | [[Category: McManus, M T | + | </StructureSection> |
| - | [[Category: Stevenson, C E.M | + | [[Category: Moss]] |
| + | [[Category: Hughes, R K]] | ||
| + | [[Category: Kopriva, S]] | ||
| + | [[Category: Lawson, D M]] | ||
| + | [[Category: McManus, M T]] | ||
| + | [[Category: Stevenson, C E.M]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Sulfate assimilation]] | [[Category: Sulfate assimilation]] | ||
[[Category: Sulfonucleotide]] | [[Category: Sulfonucleotide]] | ||
Revision as of 17:29, 21 December 2014
Structure of Adenosine 5-prime-phosphosulfate Reductase apr-b from Physcomitrella Patens
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