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5djk

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Structure of M. tuberculosis CysQ, a PAP phosphatase with PO4 and 2Ca bound

Structural highlights

5djk is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.799Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2]

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gu X, Chen M, Shen H, Jiang X, Huang Y, Wang H. Rv2131c gene product: an unconventional enzyme that is both inositol monophosphatase and fructose-1,6-bisphosphatase. Biochem Biophys Res Commun. 2006 Jan 20;339(3):897-904. PMID:16325768 doi:10.1016/j.bbrc.2005.11.088
↑ Hatzios SK, Iavarone AT, Bertozzi CR. Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase. Biochemistry. 2008 May 27;47(21):5823-31. PMID:18454554 doi:10.1021/bi702453s
↑ Erickson AI, Sarsam RD, Fisher AJ. Crystal Structures of Mycobacterium tuberculosis CysQ, with Substrate and Products Bound. Biochemistry. 2015 Nov 17;54(45):6830-41. doi: 10.1021/acs.biochem.5b01000. Epub , 2015 Nov 5. PMID:26512869 doi:http://dx.doi.org/10.1021/acs.biochem.5b01000

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5djk"

Categories: Large Structures | Mycobacterium tuberculosis | Erickson AI | Fisher AJ

@@ Line 1: / Line 1: @@
 ==Structure of M. tuberculosis CysQ, a PAP phosphatase with PO4 and 2Ca bound==
-<StructureSection load='5djk' size='340' side='right' caption='[[5djk]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='5djk' size='340' side='right'caption='[[5djk]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5djk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DJK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DJK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5djk]] 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=5DJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DJK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.799&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5djf|5djf]], [[5djj|5djj]], [[5dji|5dji]], [[5djh|5djh]], [[5djg|5djg]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5djk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djk OCA], [http://pdbe.org/5djk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5djk RCSB], [http://www.ebi.ac.uk/pdbsum/5djk PDBsum]</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=5djk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djk OCA], [https://pdbe.org/5djk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5djk RCSB], [https://www.ebi.ac.uk/pdbsum/5djk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5djk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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).
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5djk" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
+*[[Inositol monophosphatase 3D structures|Inositol monophosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Erickson, A I]]
+[[Category: Large Structures]]
-[[Category: Fisher, A J]]
+[[Category: Mycobacterium tuberculosis]]
-[[Category: Calcium]]
+[[Category: Erickson AI]]
-[[Category: Cysq]]
+[[Category: Fisher AJ]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Inhibitor]]
-[[Category: Pap phosphatase]]

5djk

From Proteopedia

Current revision

Structure of M. tuberculosis CysQ, a PAP phosphatase with PO4 and 2Ca bound

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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