6r1m: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6r1m is ~~ON HOLD until Paper~~ Publication

==Crystal structure of E. coli seryl-tRNA synthetase complexed to seryl sulfamoyl adenosine==

== Structural highlights ==

<table><tr><td colspan='2'>[[6r1m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R1M FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SSA:5-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE'>SSA</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] </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=6r1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r1m OCA], [http://pdbe.org/6r1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r1m RCSB], [http://www.ebi.ac.uk/pdbsum/6r1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r1m ProSAT]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/A0A1X3JK72_ECOLX A0A1X3JK72_ECOLX]] Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).[HAMAP-Rule:MF_00176]

== Publication Abstract from PubMed ==

Aminoacyl-tRNA synthetases are ubiquitous and essential enzymes for protein synthesis and also a variety of other metabolic processes, especially in bacterial species. Bacterial aminoacyl-tRNA synthetases represent attractive and validated targets for antimicrobial drug discovery if issues of prokaryotic versus eukaryotic selectivity and antibiotic resistance generation can be addressed. We have determined high-resolution X-ray crystal structures of the Escherichia coli and Staphylococcus aureus seryl-tRNA synthetases in complex with aminoacyl adenylate analogues and applied a structure-based drug discovery approach to explore and identify a series of small molecule inhibitors that selectively inhibit bacterial seryl-tRNA synthetases with greater than 2 orders of magnitude compared to their human homologue, demonstrating a route to the selective chemical inhibition of these bacterial targets.

~~Authors: Salimraj, R~~., Cain, R., ~~Roper~~, D.I.

Structure-Guided Enhancement of Selectivity of Chemical Probe Inhibitors Targeting Bacterial Seryl-tRNA Synthetase.,Cain R, Salimraj R, Punekar AS, Bellini D, Fishwick CWG, Czaplewski L, Scott DJ, Harris G, Dowson CG, Lloyd AJ, Roper DI J Med Chem. 2019 Nov 14;62(21):9703-9717. doi: 10.1021/acs.jmedchem.9b01131. Epub, 2019 Nov 5. PMID:31626547<ref>PMID:31626547</ref>

~~Description: Crystal structure~~ of E. ~~coli seryl~~-~~tRNA synthetase complexed to seryl sulfamoyl adenosine~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Roper, D.I~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Serine--tRNA ligase]]

[[Category: Cain, R]]

[[Category: Roper, D I]]

[[Category: Salimraj, R]]

[[Category: Aminoacyl-trna synthetase]]

[[Category: Class ii]]

[[Category: Inhibitor]]

[[Category: Ligase]]

[[Category: Protein synthesis]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6r1m is ON HOLD  until Paper Publication
+==Crystal structure of E. coli seryl-tRNA synthetase complexed to seryl sulfamoyl adenosine==
+<StructureSection load='6r1m' size='340' side='right'caption='[[6r1m]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6r1m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R1M FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SSA:5-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE'>SSA</scene></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] </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=6r1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r1m OCA], [http://pdbe.org/6r1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r1m RCSB], [http://www.ebi.ac.uk/pdbsum/6r1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r1m ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/A0A1X3JK72_ECOLX A0A1X3JK72_ECOLX]] Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).[HAMAP-Rule:MF_00176]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Aminoacyl-tRNA synthetases are ubiquitous and essential enzymes for protein synthesis and also a variety of other metabolic processes, especially in bacterial species. Bacterial aminoacyl-tRNA synthetases represent attractive and validated targets for antimicrobial drug discovery if issues of prokaryotic versus eukaryotic selectivity and antibiotic resistance generation can be addressed. We have determined high-resolution X-ray crystal structures of the Escherichia coli and Staphylococcus aureus seryl-tRNA synthetases in complex with aminoacyl adenylate analogues and applied a structure-based drug discovery approach to explore and identify a series of small molecule inhibitors that selectively inhibit bacterial seryl-tRNA synthetases with greater than 2 orders of magnitude compared to their human homologue, demonstrating a route to the selective chemical inhibition of these bacterial targets.
-Authors: Salimraj, R., Cain, R., Roper, D.I.
+Structure-Guided Enhancement of Selectivity of Chemical Probe Inhibitors Targeting Bacterial Seryl-tRNA Synthetase.,Cain R, Salimraj R, Punekar AS, Bellini D, Fishwick CWG, Czaplewski L, Scott DJ, Harris G, Dowson CG, Lloyd AJ, Roper DI J Med Chem. 2019 Nov 14;62(21):9703-9717. doi: 10.1021/acs.jmedchem.9b01131. Epub, 2019 Nov 5. PMID:31626547<ref>PMID:31626547</ref>
-Description: Crystal structure of E. coli seryl-tRNA synthetase complexed to seryl sulfamoyl adenosine
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Roper, D.I]]
+<div class="pdbe-citations 6r1m" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Serine--tRNA ligase]]
 [[Category: Cain, R]]
+[[Category: Roper, D I]]
 [[Category: Salimraj, R]]
+[[Category: Aminoacyl-trna synthetase]]
+[[Category: Class ii]]
+[[Category: Inhibitor]]
+[[Category: Ligase]]
+[[Category: Protein synthesis]]