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| | <StructureSection load='5f24' size='340' side='right'caption='[[5f24]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5f24' size='340' side='right'caption='[[5f24]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5f24]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4g60 4g60]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F24 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F24 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f24]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4g60 4g60]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F24 FirstGlance]. <br> |
| - | </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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPD:D-MYO-INOSITOL-1-PHOSPHATE'>IPD</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </span></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPD:D-MYO-INOSITOL-1-PHOSPHATE'>IPD</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=5f24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f24 OCA], [http://pdbe.org/5f24 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f24 RCSB], [http://www.ebi.ac.uk/pdbsum/5f24 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f24 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=5f24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f24 OCA], [https://pdbe.org/5f24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f24 RCSB], [https://www.ebi.ac.uk/pdbsum/5f24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f24 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2FVV7_STAA8 Q2FVV7_STAA8] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Inositol-phosphate phosphatase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhattacharyya, S]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Das, A K]] | + | [[Category: Bhattacharyya S]] |
| - | [[Category: Dutta, D]] | + | [[Category: Das AK]] |
| - | [[Category: Ghosh, A K]] | + | [[Category: Dutta D]] |
| - | [[Category: Fig superfamily]] | + | [[Category: Ghosh AK]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Impase/nadp phosphatase]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| - | [[Category: Substrate bound complex]]
| + | |
| Structural highlights
5f24 is a 2 chain structure with sequence from Staphylococcus aureus. This structure supersedes the now removed PDB entry 4g60. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.5Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q2FVV7_STAA8
Publication Abstract from PubMed
NADP(H)/NAD(H) homeostasis has long been identified to play a pivotal role in the mitigation of reactive oxygen stress (ROS) in the intracellular milieu and is therefore critical for the progression and pathogenesis of many diseases. NAD(H) kinases and NADP(H) phosphatases are two key players in this pathway. Despite structural evidence demonstrating the existence and mode of action of NAD(H) kinases, the specific annotation and the mode of action of NADP(H) phosphatases remains obscure. Here, structural evidence supporting the alternative role of inositol monophosphatase (IMPase) as an NADP(H) phosphatase is reported. Crystal structures of staphylococcal dual-specific IMPase/NADP(H) phosphatase (SaIMPase-I) in complex with the substrates D-myo-inositol-1-phosphate and NADP(+) have been solved. The structure of the SaIMPase-I-Ca(2+)-NADP(+) ternary complex reveals the catalytic mode of action of NADP(H) phosphatase. Moreover, structures of SaIMPase-I-Ca(2+)-substrate complexes have reinforced the earlier proposal that the length of the active-site-distant helix alpha4 and its preceding loop are the predisposing factors for the promiscuous substrate specificity of SaIMPase-I. Altogether, the evidence presented suggests that IMPase-family enzymes with a shorter alpha4 helix could be potential candidates for previously unreported NADP(H) phosphatase activity.
Structural elucidation of the NADP(H) phosphatase activity of staphylococcal dual-specific IMPase/NADP(H) phosphatase.,Bhattacharyya S, Dutta A, Dutta D, Ghosh AK, Das AK Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):281-90. doi:, 10.1107/S2059798316000620. Epub 2016 Jan 28. PMID:26894675[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bhattacharyya S, Dutta A, Dutta D, Ghosh AK, Das AK. Structural elucidation of the NADP(H) phosphatase activity of staphylococcal dual-specific IMPase/NADP(H) phosphatase. Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):281-90. doi:, 10.1107/S2059798316000620. Epub 2016 Jan 28. PMID:26894675 doi:http://dx.doi.org/10.1107/S2059798316000620
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