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| | <StructureSection load='3vom' size='340' side='right'caption='[[3vom]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3vom' size='340' side='right'caption='[[3vom]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vom]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VOM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vom]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VOM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fyf|2fyf]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT0907, MTCY31.12c, Rv0884c, serC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_transaminase Phosphoserine transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.52 2.6.1.52] </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=3vom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vom OCA], [https://pdbe.org/3vom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vom RCSB], [https://www.ebi.ac.uk/pdbsum/3vom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vom 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=3vom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vom OCA], [https://pdbe.org/3vom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vom RCSB], [https://www.ebi.ac.uk/pdbsum/3vom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vom ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SERC_MYCTU SERC_MYCTU]] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).[HAMAP-Rule:MF_00160]
| + | [https://www.uniprot.org/uniprot/SERC_MYCTU SERC_MYCTU] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).[HAMAP-Rule:MF_00160] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoserine transaminase]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Baker, E N]] | + | [[Category: Baker EN]] |
| - | [[Category: Baker, H M]] | + | [[Category: Baker HM]] |
| - | [[Category: Coulibaly, F]] | + | [[Category: Coulibaly F]] |
| - | [[Category: Lassalle, E]] | + | [[Category: Lassalle E]] |
| - | [[Category: Phosphoserine aminotransferase]]
| + | |
| - | [[Category: Plp-dependent enzyme]]
| + | |
| - | [[Category: Psat]]
| + | |
| - | [[Category: Serc]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
SERC_MYCTU Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).[HAMAP-Rule:MF_00160]
Publication Abstract from PubMed
Mycobacterium tuberculosis (Mtb), the causative agent of TB, remains a serious world health problem owing to limitations of the available drugs and the emergence of resistant strains. In this context, key biosynthetic enzymes from Mtb are attractive targets for the development of new therapeutic drugs. Here, the 1.5 A resolution crystal structure of Mtb phosphoserine aminotransferase (MtbPSAT) in complex with its cofactor, pyridoxal 5'-phosphate (PLP), is reported. MtbPSAT is an essential enzyme in the biosynthesis of serine and in pathways of one-carbon metabolism. The structure shows that although the Mtb enzyme differs substantially in sequence from other PSAT enzymes, its fold is conserved and its PLP-binding site is virtually identical. Structural comparisons suggest that this site remains unchanged throughout the catalytic cycle. On the other hand, PSAT enzymes are obligate dimers in which the two active sites are located in the dimer interface and distinct differences in the MtbPSAT dimer are noted. These impact on the substrate-binding region and access channel and suggest options for the development of selective inhibitors.
Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis.,Coulibaly F, Lassalle E, Baker HM, Baker EN Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):553-63. Epub 2012 Apr 17. PMID:22525753[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Coulibaly F, Lassalle E, Baker HM, Baker EN. Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):553-63. Epub 2012 Apr 17. PMID:22525753 doi:10.1107/S0907444912004829
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