5i7h: Difference between revisions

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<StructureSection load='5i7h' size='340' side='right'caption='[[5i7h]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
<StructureSection load='5i7h' size='340' side='right'caption='[[5i7h]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5i7h]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I7H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I7H FirstGlance]. <br>
<table><tr><td colspan='2'>[[5i7h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I7H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=68V:3-{[(4-BROMOPHENYL)CARBAMOYL]AMINO}BENZOIC+ACID'>68V</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2.57&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fgp|3fgp]], [[3dki|3dki]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=68V:3-{[(4-BROMOPHENYL)CARBAMOYL]AMINO}BENZOIC+ACID'>68V</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysM, Rv1336, MTCY130.21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=5i7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i7h OCA], [https://pdbe.org/5i7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i7h RCSB], [https://www.ebi.ac.uk/pdbsum/5i7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i7h 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/[CysO_sulfur-carrier_protein]-thiocarboxylate-dependent_cysteine_synthase [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.113 2.5.1.113] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5i7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i7h OCA], [http://pdbe.org/5i7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i7h RCSB], [http://www.ebi.ac.uk/pdbsum/5i7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i7h 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>  
<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: Myctu]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Maric, S]]
[[Category: Maric S]]
[[Category: Schneider, G]]
[[Category: Schneider G]]
[[Category: Schnell, R]]
[[Category: Schnell R]]
[[Category: Cysteine biosynthesis]]
[[Category: Inhibitor]]
[[Category: Lyase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Sulphur metabolism]]
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