5djf

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==Structure of M. tuberculosis CysQ, a PAP phosphatase - ligand-free structure==
==Structure of M. tuberculosis CysQ, a PAP phosphatase - ligand-free structure==
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<StructureSection load='5djf' size='340' side='right' caption='[[5djf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='5djf' size='340' side='right'caption='[[5djf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5djf]] is a 1 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=5DJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DJF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5djf]] is a 1 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=5DJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DJF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5djj|5djj]], [[5dji|5dji]], [[5djh|5djh]], [[5djg|5djg]], [[5djk|5djk]]</td></tr>
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<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=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysQ, MT2189 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5djf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djf OCA], [https://pdbe.org/5djf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5djf RCSB], [https://www.ebi.ac.uk/pdbsum/5djf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5djf ProSAT]</span></td></tr>
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<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=5djf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djf OCA], [http://pdbe.org/5djf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5djf RCSB], [http://www.ebi.ac.uk/pdbsum/5djf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5djf ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CYSQ_MYCTO CYSQ_MYCTO]] Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might has no significance in vivo (By similarity).
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[https://www.uniprot.org/uniprot/CYSQ_MYCTU CYSQ_MYCTU] Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might not be significant in vivo. Glucose-1-phosphate (G-1-P), p-nitrophenyl phosphate (pNPP), and beta-glycerol phosphate (beta-GP) are also good substrates, compared to I-1-P. With much lower efficiency, can also hydrolyze inositol 2-phosphate (I-2-P) and glucose-6-phosphate (G-6-P) in vitro, but not fructose-6-phosphate (F-6-P) and trehalose-6-phosphate (T-6-P).<ref>PMID:16325768</ref> <ref>PMID:18454554</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In many organisms, 3'-phosphoadenosine 5'-phosphate (PAP) is a product of two reactions in the sulfur activation pathway. The sulfurylation of biomolecules, catalyzed by sulfotransferases, uses 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a sulfate donor, producing the sulfated biomolecule and PAP product. Additionally, the first step in sulfate reduction for many bacteria and fungi reduces the sulfate moiety of PAPS, producing PAP and sulfite, which is subsequently reduced to sulfide. PAP is removed by the phosphatase activity of CysQ, a 3',5'-bisphosphate nucleotidase, yielding AMP and phosphate. Because excess PAP alters the equilibrium of the sulfur pathway and inhibits sulfotransferases, PAP concentrations can affect the levels of sulfur-containing metabolites. Therefore, CysQ, a divalent cation metal-dependent phosphatase, is a major regulator of this pathway. CysQ (Rv2131c) from Mycobacterium tuberculosis (Mtb) was successfully expressed, purified, and crystallized in a variety of ligand-bound states. Here we report six crystal structures of Mtb CysQ, including a ligand-free structure, a lithium-inhibited state with substrate PAP bound, and a product-bound complex with AMP, phosphate, and three Mg(2+) ions bound. Comparison of these structures together with homologues of the superfamily has provided insight into substrate specificity, metal coordination, and catalytic mechanism.
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Crystal Structures of Mycobacterium tuberculosis CysQ, with Substrate and Products Bound.,Erickson AI, Sarsam RD, Fisher AJ Biochemistry. 2015 Nov 17;54(45):6830-41. doi: 10.1021/acs.biochem.5b01000. Epub , 2015 Nov 5. PMID:26512869<ref>PMID:26512869</ref>
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==See Also==
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*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Inositol monophosphatase 3D structures|Inositol monophosphatase 3D structures]]
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</div>
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<div class="pdbe-citations 5djf" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Erickson, A I]]
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[[Category: Large Structures]]
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[[Category: Fisher, A J]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Apo-enzyme]]
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[[Category: Erickson AI]]
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[[Category: Cysq]]
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[[Category: Fisher AJ]]
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[[Category: Hydrolase]]
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[[Category: Pap phosphatase]]
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Structure of M. tuberculosis CysQ, a PAP phosphatase - ligand-free structure

PDB ID 5djf

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