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| | ==Crystal strucuture of an inositol monophosphatase family protein (SAS2203) from Staphylococcus aureus MSSA476== | | ==Crystal strucuture of an inositol monophosphatase family protein (SAS2203) from Staphylococcus aureus MSSA476== |
| - | <StructureSection load='3qmf' size='340' side='right' caption='[[3qmf]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3qmf' size='340' side='right'caption='[[3qmf]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qmf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mssa476 Staphylococcus aureus subsp. aureus mssa476]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QMF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qmf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MSSA476 Staphylococcus aureus subsp. aureus MSSA476]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QMF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ryd|3ryd]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAS2203 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=282459 Staphylococcus aureus subsp. aureus MSSA476])</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=3qmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmf OCA], [https://pdbe.org/3qmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qmf RCSB], [https://www.ebi.ac.uk/pdbsum/3qmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmf 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/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>
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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=3qmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qmf RCSB], [http://www.ebi.ac.uk/pdbsum/3qmf PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3qmf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Inositol monophosphatase 3D structures|Inositol monophosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Inositol-phosphate phosphatase]] | + | [[Category: Large Structures]] |
| - | [[Category: Staphylococcus aureus subsp. aureus mssa476]] | + | [[Category: Staphylococcus aureus subsp. aureus MSSA476]] |
| - | [[Category: Bhattacharyya, S]] | + | [[Category: Bhattacharyya S]] |
| - | [[Category: Das, A K]] | + | [[Category: Das AK]] |
| - | [[Category: Dutta, D]] | + | [[Category: Dutta D]] |
| - | [[Category: Ghosh, A K]] | + | [[Category: Ghosh AK]] |
| - | [[Category: Fig superfamily]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Impase fold]]
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| Structural highlights
Publication Abstract from PubMed
Inositol monophosphatase (IMPase) family of proteins are Mg(2+) activated Li(+) inhibited class of ubiquitous enzymes with promiscuous substrate specificity. Herein, the molecular basis of IMPase substrate specificity is delineated by comparative crystal structural analysis of a Staphylococcal dual specific IMPase/NADP(H) phosphatase (SaIMPase - I) with other IMPases of different substrate compatibility, empowered by in silico docking and Escherichiacoli SuhB mutagenesis analysis. Unlike its eubacterial and eukaryotic NADP(H) non-hydrolyzing counterparts, the composite structure of SaIMPase - I active site pocket exhibits high structural resemblance with archaeal NADP(H) hydrolyzing dual specific IMPase/FBPase. The large and shallow SaIMPase - I active site cleft efficiently accommodate large incoming substrates like NADP(H), and therefore, justifies the eminent NADP(H) phosphatase activity of SaIMPase - I. Compared to other NADP(H) non-hydrolyzing IMPases, the profound difference in active site topology as well as the unique NADP(H) recognition capability of SaIMPase - I stems from the differential length and orientation of a distant helix alpha4 (in human and bovine alpha5) and its preceding loop. We identified the length of alpha4 and its preceding loop as the most crucial factor that regulates IMPase substrate specificity by employing a size exclusion mechanism. Hence, in SaIMPase - I, the substrate promiscuity is a gain of function by trimming the length of alpha4 and its preceding loop, compared to other NADP(H) non-hydrolyzing IMPases. This study thus provides a biochemical - structural framework revealing the length and orientation of alpha4 and its preceding loop as the predisposing factor for the determination of IMPase substrate specificity.
Crystal structure of Staphylococcal dual specific inositol monophosphatase/NADP(H) phosphatase (SAS2203) delineates the molecular basis of substrate specificity.,Bhattacharyya S, Dutta D, Saha B, Ghosh AK, Das AK Biochimie. 2011 Dec 16. PMID:22197784[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bhattacharyya S, Dutta D, Saha B, Ghosh AK, Das AK. Crystal structure of Staphylococcal dual specific inositol monophosphatase/NADP(H) phosphatase (SAS2203) delineates the molecular basis of substrate specificity. Biochimie. 2011 Dec 16. PMID:22197784 doi:10.1016/j.biochi.2011.12.007
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