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| | ==Crystal structure of PLP bound phosphoserine aminotransferase (PSAT) from Trichomonas vaginalis== | | ==Crystal structure of PLP bound phosphoserine aminotransferase (PSAT) from Trichomonas vaginalis== |
| - | <StructureSection load='5f8v' size='340' side='right' caption='[[5f8v]], [[Resolution|resolution]] 2.14Å' scene=''> | + | <StructureSection load='5f8v' size='340' side='right'caption='[[5f8v]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5f8v]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Triva Triva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F8V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f8v]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F8V FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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]] 2.14Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TVAG_224040 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5722 TRIVA])</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></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=5f8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8v OCA], [http://pdbe.org/5f8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8v RCSB], [http://www.ebi.ac.uk/pdbsum/5f8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8v 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=5f8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8v OCA], [https://pdbe.org/5f8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f8v RCSB], [https://www.ebi.ac.uk/pdbsum/5f8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A2DW27_TRIV3 A2DW27_TRIV3] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5f8v" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5f8v" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Triva]] | + | [[Category: Large Structures]] |
| - | [[Category: Gourinath, S]] | + | [[Category: Trichomonas vaginalis]] |
| - | [[Category: Singh, R K]] | + | [[Category: Gourinath S]] |
| - | [[Category: Alpha-beta domain]] | + | [[Category: Singh RK]] |
| - | [[Category: Alpha-family]]
| + | |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A2DW27_TRIV3
Publication Abstract from PubMed
BACKGROUND: Phosphoserine aminotransferase (PSAT) catalyses the second reversible step of the phosphoserine biosynthetic pathway in Trichomonas vaginalis, which is crucial for the synthesis of serine and cysteine. METHODS: PSAT from T. vaginalis (TvPSAT) was analysed using X-ray crystallography, enzyme kinetics, and molecular dynamics simulations. RESULTS: The crystal structure of TvPSAT was determined to 2.15A resolution, and is the first protozoan PSAT structure to be reported. The active site of TvPSAT structure was found to be in a closed conformation, and at the active site PLP formed an internal aldimine linkage to Lys 202. In TvPSAT, Val 340 near the active site while it is Arg in most other members of the PSAT family, might be responsible in closing the active site. Kinetic studies yielded Km values of 54 muM and 202 muM for TvPSAT with OPLS and AKG, respectively. Only iodine inhibited the TvPSAT activity while smaller halides could not inhibit. CONCLUSION: Results from the structure, comparative molecular dynamics simulations, and the inhibition studies suggest that iodine is the only halide that can bind TvPSAT strongly and may thus inhibit the activity of TvPSAT. The long loop between beta8 and alpha8 at the opening of the TvPSAT active site cleft compared to other PSATs, suggests that this loop may help control the access of substrates to the TvPSAT active site and thus influences the enzyme kinetics. GENERAL SIGNIFICANCE: Our structural and functional studies have improved our understanding of how PSAT helps this organism persists in the environment.
Structural investigation and inhibitory response of halide on phosphoserine aminotransferase from Trichomonas vaginalis.,Singh RK, Mazumder M, Sharma B, Gourinath S Biochim Biophys Acta. 2016 Jul;1860(7):1508-18. doi:, 10.1016/j.bbagen.2016.04.013. Epub 2016 Apr 19. PMID:27102280[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Singh RK, Mazumder M, Sharma B, Gourinath S. Structural investigation and inhibitory response of halide on phosphoserine aminotransferase from Trichomonas vaginalis. Biochim Biophys Acta. 2016 Jul;1860(7):1508-18. doi:, 10.1016/j.bbagen.2016.04.013. Epub 2016 Apr 19. PMID:27102280 doi:http://dx.doi.org/10.1016/j.bbagen.2016.04.013
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