7lhs: Difference between revisions

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New page: '''Unreleased structure''' The entry 7lhs is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 7lhs is ON HOLD
==Crystal structure of adenosine-5'-phosphosulfate reductase from Mycobacterium tuberculosis in a complex with substrate APS==
<StructureSection load='7lhs' size='340' side='right'caption='[[7lhs]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LHS 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]] 3.11&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADX:ADENOSINE-5-PHOSPHOSULFATE'>ADX</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=7lhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lhs OCA], [https://pdbe.org/7lhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lhs RCSB], [https://www.ebi.ac.uk/pdbsum/7lhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lhs ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tuberculosis (TB) is the deadliest infectious disease in the world. In Mycobacterium tuberculosis, the first committed step in sulfate assimilation is the reductive cleavage of adenosine-5'-phosphosulfate (APS) to form adenosine-5'-phosphate (AMP) and sulfite by the enzyme APS reductase (APSR). The vital role of APSR in the production of essential reduced-sulfur-containing metabolites and the absence of a homologue enzyme in humans makes APSR a potential target for therapeutic interventions. Here, we present the crystal structure of the [4Fe-4S] cluster-containing APSR from M. tuberculosis (MtbAPSR) and compare it to previously determined structures of sulfonucleotide reductases. We further present MtbAPSR structures with substrate APS and product AMP bound in the active site. Our structures at a 3.1 A resolution show high structural similarity to other sulfonucleotide reductases and reveal that APS and AMP have similar binding modes. These studies provide structural data for structure-based drug design aimed to combat TB.


Authors:  
Crystal Structure of the [4Fe-4S] Cluster-Containing Adenosine-5'-phosphosulfate Reductase from Mycobacterium tuberculosis.,Feliciano PR, Carroll KS, Drennan CL ACS Omega. 2021 May 17;6(21):13756-13765. doi: 10.1021/acsomega.1c01043., eCollection 2021 Jun 1. PMID:34095667<ref>PMID:34095667</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7lhs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Drennan CL]]
[[Category: Feliciano PR]]

Latest revision as of 14:25, 13 August 2026

Crystal structure of adenosine-5'-phosphosulfate reductase from Mycobacterium tuberculosis in a complex with substrate APS

7lhs, resolution 3.11Å

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