5b19: Difference between revisions
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<StructureSection load='5b19' size='340' side='right'caption='[[5b19]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5b19' size='340' side='right'caption='[[5b19]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5b19]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5b19]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Picrophilus_torridus_DSM_9790 Picrophilus torridus DSM 9790]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B19 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=5b19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b19 OCA], [https://pdbe.org/5b19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b19 RCSB], [https://www.ebi.ac.uk/pdbsum/5b19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b19 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6L2R8_PICTO Q6L2R8_PICTO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Picrophilus torridus DSM 9790]] | ||
[[Category: Aihara | [[Category: Aihara T]] | ||
[[Category: Homma | [[Category: Homma H]] | ||
[[Category: Ito | [[Category: Ito T]] | ||
[[Category: Noguchi | [[Category: Noguchi K]] | ||
[[Category: Odaka | [[Category: Odaka M]] | ||
[[Category: Sekine | [[Category: Sekine M]] | ||
[[Category: Yamanaka | [[Category: Yamanaka Y]] | ||
[[Category: Yohda | [[Category: Yohda M]] | ||
Revision as of 09:34, 31 May 2023
Picrophilus torridus aspartate racemasePicrophilus torridus aspartate racemase
Structural highlights
FunctionPublication Abstract from PubMedFunctional and structural characterizations of pyridoxal 5'-phosphate-independent aspartate racemase of the acidothermophilic archaeon Picrophilus torridus were performed. Picrophilus aspartate racemase exhibited high substrate specificity to aspartic acid. The optimal reaction temperature was 60 degrees C, which is almost the same as the optimal growth temperature. Reflecting the low pH in the cytosol, the optimal reaction pH of Picrophilus aspartate racemase was approximately 5.5. However, the activity at the putative cytosolic pH of 4.6 was approximately 6 times lower than that at the optimal pH of 5.5. The crystal structure of Picrophilus aspartate racemase was almost the same as that of other pyridoxal 5'-phosphate -independent aspartate racemases. In two molecules of the dimer, one molecule contained a tartaric acid molecule in the catalytic site; the structure of the other molecule was relatively flexible. Finally, we examined the intracellular existence of D-amino acids. Unexpectedly, the proportion of D-aspartate to total aspartate was not very high. In contrast, both D-proline and D-alanine were observed. Because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus. Structural and functional characterization of aspartate racemase from the acidothermophilic archaeon Picrophilus torridus.,Aihara T, Ito T, Yamanaka Y, Noguchi K, Odaka M, Sekine M, Homma H, Yohda M Extremophiles. 2016 Apr 19. PMID:27094682[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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