7yqa: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7yqa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YQA FirstGlance]. <br> | <table><tr><td colspan='2'>[[7yqa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YQA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7yqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yqa OCA], [https://pdbe.org/7yqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yqa RCSB], [https://www.ebi.ac.uk/pdbsum/7yqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yqa ProSAT]</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=7yqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yqa OCA], [https://pdbe.org/7yqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yqa RCSB], [https://www.ebi.ac.uk/pdbsum/7yqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yqa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 21:11, 29 November 2023
Crystal structure of D-threonine aldolase from Chlamydomonas reinhardtiiCrystal structure of D-threonine aldolase from Chlamydomonas reinhardtii
Structural highlights
FunctionPublication Abstract from PubMedD-Threonine aldolase (DTA) is a pyridoxal-5'-phosphate-dependent enzyme which catalyzes the reversible aldol reaction of glycine with a corresponding aldehyde to yield the D-form beta-hydroxy-alpha-amino acid. This study produced and investigated the crystal structure of DTA from Chlamydomonas reinhardtii (CrDTA) at 1.85 A resolution. To our knowledge, this is the first report on the crystal structure of eukaryotic DTA. Compared with the structure of bacterial DTA, CrDTA has a similar arrangement of active-site residues. On the other hand, we speculated that some non-conserved residues alter the affinity for substrates and inhibitors. The structure of CrDTA could provide insights into the structural framework for structure-guided protein engineering studies to modify reaction selectivity. Structure of pyridoxal 5'-phosphate-bound D-threonine aldolase from Chlamydomonas reinhardtii.,Hirato Y, Goto M, Mizobuchi T, Muramatsu H, Tanigawa M, Nishimura K Acta Crystallogr F Struct Biol Commun. 2023 Feb 1;79(Pt 2):31-37. doi: , 10.1107/S2053230X23000304. Epub 2023 Feb 2. PMID:36748339[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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