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4bwv
From Proteopedia
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| - | {{STRUCTURE_4bwv| PDB=4bwv | SCENE= }} | ||
| - | ===Structure of Adenosine 5-prime-phosphosulfate Reductase apr-b from Physcomitrella Patens=== | ||
| - | {{ABSTRACT_PUBMED_24100135}} | ||
| - | == | + | ==Structure of Adenosine 5-prime-phosphosulfate Reductase apr-b from Physcomitrella Patens== |
| - | [[4bwv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWV OCA]. | + | <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 [https://en.wikipedia.org/wiki/Physcomitrium_patens Physcomitrium patens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4BWV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=4bwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwv OCA], [https://pdbe.org/4bwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bwv RCSB], [https://www.ebi.ac.uk/pdbsum/4bwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8L5D0_PHYPA Q8L5D0_PHYPA] | ||
| + | <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> | |
| - | <ref | + | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4bwv" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Physcomitrium patens]] | ||
| + | [[Category: Hughes RK]] | ||
| + | [[Category: Kopriva S]] | ||
| + | [[Category: Lawson DM]] | ||
| + | [[Category: McManus MT]] | ||
| + | [[Category: Stevenson CEM]] | ||
Current revision
Structure of Adenosine 5-prime-phosphosulfate Reductase apr-b from Physcomitrella Patens
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