|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5xcn' size='340' side='right'caption='[[5xcn]], [[Resolution|resolution]] 1.69Å' scene=''> | | <StructureSection load='5xcn' size='340' side='right'caption='[[5xcn]], [[Resolution|resolution]] 1.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xcn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haein Haein]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XCN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xcn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XCN 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]] 1.69Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5xcp|5xcp]], [[5xcw|5xcw]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysK, HI_1103 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </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=5xcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xcn OCA], [https://pdbe.org/5xcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xcn RCSB], [https://www.ebi.ac.uk/pdbsum/5xcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xcn 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=5xcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xcn OCA], [https://pdbe.org/5xcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xcn RCSB], [https://www.ebi.ac.uk/pdbsum/5xcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xcn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CYSK_HAEIN CYSK_HAEIN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cysteine synthase]] | + | [[Category: Haemophilus influenzae Rd KW20]] |
| - | [[Category: Haein]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abhishek, K]] | + | [[Category: Abhishek K]] |
| - | [[Category: Kumaran, S]] | + | [[Category: Kumaran S]] |
| - | [[Category: Cysteine synthase activity]]
| + | |
| - | [[Category: L-cysteine desulfhydrase activity]]
| + | |
| - | [[Category: Pyridoxal phosphate binding]]
| + | |
| - | [[Category: Serine acetyl transferase interacting protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase activity]]
| + | |
| Structural highlights
Function
CYSK_HAEIN
Publication Abstract from PubMed
O-acetyl serine sulfhydrylase (OASS), referred to as Cysteine Synthase (CS), synthesizes cysteine from O-acetyl serine (OAS) and sulfur in bacteria and plants. The inherent challenge for CS is to overcome 4-6 log-folds stronger affinity for its natural inhibitor, serine acetyltransferase (SAT), as compared to its affinity for substrate, OAS. Our recent study showed that CS employs a novel competitive-allosteric mechanism to selectively recruit its substrate in the presence of natural inhibitor [1]. In this study, we trace the molecular features that control selective substrate recruitment. To generalize our findings, we used CS from three different bacteria (Haemophilus, Salmonella, and Mycobacterium) as our model systems and analysed structural and substrate-binding features of wild type CS and its ~13 mutants. Results show that CS uses a non-catalytic residue, M120, located 20 A away from the reaction centre, to discriminate in favour of substrate. M120A and background mutants display significantly reduced substrate binding, catalytic efficiency, and inhibitor binding. Results shows that M120 favours the substrate binding by selectively enhancing the affinity for the substrate and dis-engaging the inhibitor by 20-286 and 5-3 folds respectively. Together, M120 confers a net discriminative force in favour of substrate by 100-858 folds.
Molecular Mechanism of Selective Substrate Engagement and Inhibitor Dis-engagement of Cysteine Synthase.,Kaushik A, Rahisuddin R, Saini N, Singh RP, Kaur R, Kaul S, Kumaran S J Biol Chem. 2020 Nov 8. pii: S0021-9258(20)00027-7. doi:, 10.1074/jbc.RA120.014490. PMID:33162395[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaushik A, Rahisuddin R, Saini N, Singh RP, Kaur R, Kaul S, Kumaran S. Molecular Mechanism of Selective Substrate Engagement and Inhibitor Dis-engagement of Cysteine Synthase. J Biol Chem. 2020 Nov 8. pii: S0021-9258(20)00027-7. doi:, 10.1074/jbc.RA120.014490. PMID:33162395 doi:http://dx.doi.org/10.1074/jbc.RA120.014490
|
