4h27
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4h27 is ON HOLD Authors: Wang, C.Y., Wang, A.H. Description: Modulating the function of human serine racemase and human serine dehydratase by prote...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Modulating the function of human serine racemase and human serine dehydratase by protein engineering== | |
| + | <StructureSection load='4h27' size='340' side='right'caption='[[4h27]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4h27]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H27 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]] 1.3Å</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=SO4:SULFATE+ION'>SO4</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=4h27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h27 OCA], [https://pdbe.org/4h27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h27 RCSB], [https://www.ebi.ac.uk/pdbsum/4h27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h27 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SDHL_HUMAN SDHL_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | d-Serine is a co-agonist of N-methyl d-aspartate, a glutamate receptor, which is a major excitatory neurotransmitter receptor in the brain. Human serine racemase (hSR) and serine dehydratase (hSDH) are two important pyridoxal-5'-phosphate-dependent enzymes that synthesize and degrade d-serine, respectively. hSR and hSDH have significant sequence homology (28% identity) and are similar in their structural folds (root-mean-square deviation, 1.12 A). Sequence alignment and structural comparison between hSR and hSDH reveal that S84 in hSR and A65 in hSDH play important roles in their respective enzyme activities. We surmise that exchange of these two amino acids by introducing S84A hSR and A65S hSDH mutants may result in switching their protein functions. To understand the modulating mechanism of the key residues, mutants S84A in hSR and A65S in hSDH were constructed to monitor the change of activities. The structure of A65S hSDH mutant was determined at 1.3 A resolution (PDB 4H27), elucidating the role of this critical amino acid. Our study demonstrated S84A hSR mutant behaved like hSDH, whereas A65S hSDH mutant acquired an additional function of using d-serine as a substrate. | ||
| - | + | Modulating the function of human serine racemase and human serine dehydratase by protein engineering.,Wang CY, Ku SC, Lee CC, Wang AH Protein Eng Des Sel. 2012 Nov;25(11):741-9. doi: 10.1093/protein/gzs078. Epub, 2012 Oct 30. PMID:23112234<ref>PMID:23112234</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4h27" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Wang AH]] | ||
| + | [[Category: Wang CY]] | ||
Current revision
Modulating the function of human serine racemase and human serine dehydratase by protein engineering
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