8yrv: Difference between revisions
New page: '''Unreleased structure''' The entry 8yrv is ON HOLD Authors: Matyuta, I.O., Bakunova, A.K., Nikolaeva, A.Y., Popov, V.O., Boyko, K.M. Description: Crystal structure of D-amino acid tr... |
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==Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acid== | |||
<StructureSection load='8yrv' size='340' side='right'caption='[[8yrv]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8yrv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliscomenobacter_hydrossis_DSM_1100 Haliscomenobacter hydrossis DSM 1100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YRV 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OCF:3-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxypropanoic+acid'>OCF</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=8yrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yrv OCA], [https://pdbe.org/8yrv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yrv RCSB], [https://www.ebi.ac.uk/pdbsum/8yrv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yrv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/F4KWH0_HALH1 F4KWH0_HALH1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pyridoxal 5'-phosphate-dependent enzymes play a crucial role in nitrogen metabolism. Carbonyl compounds, such as O-substituted hydroxylamines, stand out among numerous specific inhibitors of these enzymes, including those of practical importance, because they react with pyridoxal 5'-phosphate in the active site of the enzymes to form stable oximes. O-substituted hydroxylamines mimic the side group of amino acid substrates, thus providing highly potent and specific inhibition of the corresponding enzymes. The interaction between D-amino acid transaminase from bacterium Haliscomenobacter hydrossis and 3-aminooxypropionic acid was studied in the present work. The structural and spectral analyses of the complex of this transaminase with 3-aminooxypropionic acid allowed us to clarify some features of the organization and functioning of its active site and illustrate one of the mechanisms of inhibition by the specific substrate, D-glutamic acid. | |||
Insights into the Functioning of the D-amino Acid Transaminase from Haliscomenobacter Hydrossis via a Structural and Spectral Analysis of its Complex with 3-Aminooxypropionic Acid.,Bakunova AK, Matyuta IO, Nikolaeva AY, Boyko KM, Khomutov AR, Bezsudnova EY, Popov VO Acta Naturae. 2024 Jul-Sep;16(3):18-24. doi: 10.32607/actanaturae.27496. PMID:39539521<ref>PMID:39539521</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8yrv" style="background-color:#fffaf0;"></div> | ||
[[Category: Boyko | == References == | ||
[[Category: | <references/> | ||
[[Category: Nikolaeva | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Haliscomenobacter hydrossis DSM 1100]] | |||
[[Category: Large Structures]] | |||
[[Category: Bakunova AK]] | |||
[[Category: Boyko KM]] | |||
[[Category: Matyuta IO]] | |||
[[Category: Nikolaeva AY]] | |||
[[Category: Popov VO]] | |||
Latest revision as of 09:40, 18 December 2024
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acidCrystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acid
Structural highlights
FunctionPublication Abstract from PubMedPyridoxal 5'-phosphate-dependent enzymes play a crucial role in nitrogen metabolism. Carbonyl compounds, such as O-substituted hydroxylamines, stand out among numerous specific inhibitors of these enzymes, including those of practical importance, because they react with pyridoxal 5'-phosphate in the active site of the enzymes to form stable oximes. O-substituted hydroxylamines mimic the side group of amino acid substrates, thus providing highly potent and specific inhibition of the corresponding enzymes. The interaction between D-amino acid transaminase from bacterium Haliscomenobacter hydrossis and 3-aminooxypropionic acid was studied in the present work. The structural and spectral analyses of the complex of this transaminase with 3-aminooxypropionic acid allowed us to clarify some features of the organization and functioning of its active site and illustrate one of the mechanisms of inhibition by the specific substrate, D-glutamic acid. Insights into the Functioning of the D-amino Acid Transaminase from Haliscomenobacter Hydrossis via a Structural and Spectral Analysis of its Complex with 3-Aminooxypropionic Acid.,Bakunova AK, Matyuta IO, Nikolaeva AY, Boyko KM, Khomutov AR, Bezsudnova EY, Popov VO Acta Naturae. 2024 Jul-Sep;16(3):18-24. doi: 10.32607/actanaturae.27496. PMID:39539521[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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