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| | ==2.05 a Crystal Structure of CysM from Mycobacterium Tuberculosis - Open and Closed Conformations== | | ==2.05 a Crystal Structure of CysM from Mycobacterium Tuberculosis - Open and Closed Conformations== |
| - | <StructureSection load='3fgp' size='340' side='right' caption='[[3fgp]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='3fgp' size='340' side='right'caption='[[3fgp]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fgp]] is a 2 chain structure with sequence from [http://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=3FGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FGP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fgp]] 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=3FGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FGP 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]] 2.05Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dki|3dki]]</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">cysM (Rv1336) ([http://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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fgp OCA], [https://pdbe.org/3fgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fgp RCSB], [https://www.ebi.ac.uk/pdbsum/3fgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fgp ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/O-phosphoserine_sulfhydrylase O-phosphoserine sulfhydrylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.65 2.5.1.65] </span></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=3fgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fgp OCA], [http://pdbe.org/3fgp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fgp RCSB], [http://www.ebi.ac.uk/pdbsum/3fgp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fgp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYSM_MYCTU CYSM_MYCTU]] Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro-benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis.<ref>PMID:18842002</ref> <ref>PMID:18799456</ref> | + | [https://www.uniprot.org/uniprot/CYSM_MYCTU CYSM_MYCTU] Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro-benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis.<ref>PMID:18842002</ref> <ref>PMID:18799456</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: O-phosphoserine sulfhydrylase]] | + | [[Category: Large Structures]] |
| - | [[Category: Agren, D]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Schneider, G]] | + | [[Category: Agren D]] |
| - | [[Category: Schnell, R]] | + | [[Category: Schneider G]] |
| - | [[Category: Amino-acid biosynthesis]] | + | [[Category: Schnell R]] |
| - | [[Category: Cysm]]
| + | |
| - | [[Category: Cyso]]
| + | |
| - | [[Category: Cysteine biosynthesis]]
| + | |
| - | [[Category: Cysteine synthase]]
| + | |
| - | [[Category: O-phosphoserine]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Tuberculosis]]
| + | |
| Structural highlights
Function
CYSM_MYCTU Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro-benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A new crystal structure of the dimeric cysteine synthase CysM from Mycobacterium tuberculosis reveals an open and a closed conformation of the enzyme. In the closed conformation the five carboxy-terminal amino acid residues are inserted into the active site cleft. Removal of this segment results in a decreased lifetime of the alpha-aminoacrylate reaction intermediate, an increased sensitivity to oxidants such as hydrogen peroxide, and loss of substrate selectivity with respect to the sulfur carrier thiocarboxylated CysO. These results highlight features of CysM that might be of particular importance for cysteine biosynthesis under oxidative stress in M. tuberculosis.
The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity.,Agren D, Schnell R, Schneider G FEBS Lett. 2009 Jan 22;583(2):330-6. Epub 2008 Dec 26. PMID:19101553[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ O'Leary SE, Jurgenson CT, Ealick SE, Begley TP. O-phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis. Biochemistry. 2008 Nov 4;47(44):11606-15. doi: 10.1021/bi8013664. Epub 2008 Oct, 9. PMID:18842002 doi:http://dx.doi.org/10.1021/bi8013664
- ↑ Agren D, Schnell R, Oehlmann W, Singh M, Schneider G. Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria. J Biol Chem. 2008 Nov 14;283(46):31567-74. Epub 2008 Sep 16. PMID:18799456 doi:10.1074/jbc.M804877200
- ↑ Agren D, Schnell R, Schneider G. The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity. FEBS Lett. 2009 Jan 22;583(2):330-6. Epub 2008 Dec 26. PMID:19101553 doi:10.1016/j.febslet.2008.12.019
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