4bwv: Difference between revisions

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<StructureSection load='4bwv' size='340' side='right'caption='[[4bwv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4bwv' size='340' side='right'caption='[[4bwv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== 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>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
</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='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'>[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>
<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://pdbe.org/4bwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bwv RCSB], [http://www.ebi.ac.uk/pdbsum/4bwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwv ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[[https://www.uniprot.org/uniprot/Q8L5D0_PHYPA Q8L5D0_PHYPA]]
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bwv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Moss]]
[[Category: Physcomitrium patens]]
[[Category: Hughes, R K]]
[[Category: Hughes RK]]
[[Category: Kopriva, S]]
[[Category: Kopriva S]]
[[Category: Lawson, D M]]
[[Category: Lawson DM]]
[[Category: McManus, M T]]
[[Category: McManus MT]]
[[Category: Stevenson, C E.M]]
[[Category: Stevenson CEM]]
[[Category: Oxidoreductase]]
[[Category: Sulfate assimilation]]
[[Category: Sulfonucleotide]]

Revision as of 17:14, 7 September 2022

Structure of Adenosine 5-prime-phosphosulfate Reductase apr-b from Physcomitrella Patens

4bwv, resolution 1.80Å

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