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6g59
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6g59 is ON HOLD Authors: Hoegl, A., Sieber, S.A., Schneider, S. Description: Structure of the alanine racemase from Staphylococcus aureus without [...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the alanine racemase from Staphylococcus aureus in complex with an pyridoxal-6- phosphate derivative== | |
| + | <StructureSection load='6g59' size='340' side='right' caption='[[6g59]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6g59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G59 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EM2:(6-ethynyl-4-methanoyl-5-oxidanyl-pyridin-3-yl)methyl+dihydrogen+phosphate'>EM2</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr1, alr, SAV2070 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 STAAM])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine_racemase Alanine racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.1 5.1.1.1] </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=6g59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g59 OCA], [http://pdbe.org/6g59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g59 RCSB], [http://www.ebi.ac.uk/pdbsum/6g59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g59 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ALR1_STAAM ALR1_STAAM]] Catalyzes the interconversion of L-alanine and D-alanine.<ref>PMID:22194336</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pyridoxal phosphate (PLP) is an enzyme cofactor required for the chemical transformation of biological amines in many central cellular processes. PLP-dependent enzymes (PLP-DEs) are ubiquitous and evolutionarily diverse, making their classification based on sequence homology challenging. Here we present a chemical proteomic method for reporting on PLP-DEs using functionalized cofactor probes. We synthesized pyridoxal analogues modified at the 2'-position, which are taken up by cells and metabolized in situ. These pyridoxal analogues are phosphorylated to functional cofactor surrogates by cellular pyridoxal kinases and bind to PLP-DEs via an aldimine bond which can be rendered irreversible by NaBH4 reduction. Conjugation to a reporter tag enables the subsequent identification of PLP-DEs using quantitative, label-free mass spectrometry. Using these probes we accessed a significant portion of the Staphylococcus aureus PLP-DE proteome (73%) and annotate uncharacterized proteins as novel PLP-DEs. We also show that this approach can be used to study structural tolerance within PLP-DE active sites and to screen for off-targets of the PLP-DE inhibitor D-cycloserine. | ||
| - | + | Mining the cellular inventory of pyridoxal phosphate-dependent enzymes with functionalized cofactor mimics.,Hoegl A, Nodwell MB, Kirsch VC, Bach NC, Pfanzelt M, Stahl M, Schneider S, Sieber SA Nat Chem. 2018 Oct 8. pii: 10.1038/s41557-018-0144-2. doi:, 10.1038/s41557-018-0144-2. PMID:30297752<ref>PMID:30297752</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6g59" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Alanine racemase]] | ||
| + | [[Category: Staam]] | ||
[[Category: Hoegl, A]] | [[Category: Hoegl, A]] | ||
[[Category: Schneider, S]] | [[Category: Schneider, S]] | ||
| + | [[Category: Sieber, S A]] | ||
| + | [[Category: Biosynthetic protein]] | ||
| + | [[Category: D-alanine biosynthesis]] | ||
| + | [[Category: Pyridoxal 5 phosphate dependent]] | ||
Current revision
Structure of the alanine racemase from Staphylococcus aureus in complex with an pyridoxal-6- phosphate derivative
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