|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | ==CRYSTAL STRUCTURE OF THE PPM SER-THR PHOSPHATASE MSPP FROM MYCOBACTERIUM SMEGMATIS AT PH 5.5== | + | |
| - | <StructureSection load='2v06' size='340' side='right' caption='[[2v06]], [[Resolution|resolution]] 1.05Å' scene=''> | + | ==Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis at pH 5.5== |
| | + | <StructureSection load='2v06' size='340' side='right'caption='[[2v06]], [[Resolution|resolution]] 1.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v06]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_smegmatis"_trevisan_1889 "bacillus smegmatis" trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V06 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v06]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V06 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.05Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jfr|2jfr]], [[2jfs|2jfs]], [[2jft|2jft]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2v06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v06 OCA], [http://pdbe.org/2v06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v06 RCSB], [http://www.ebi.ac.uk/pdbsum/2v06 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=2v06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v06 OCA], [https://pdbe.org/2v06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v06 RCSB], [https://www.ebi.ac.uk/pdbsum/2v06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v06 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0QTQ6_MYCS2 A0QTQ6_MYCS2] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/2v06_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/2v06_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| Line 30: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus smegmatis trevisan 1889]] | + | [[Category: Large Structures]] |
| - | [[Category: Alzari, P M]] | + | [[Category: Mycolicibacterium smegmatis]] |
| - | [[Category: Bellinzoni, M]] | + | [[Category: Alzari PM]] |
| - | [[Category: Schaeffer, F]] | + | [[Category: Bellinzoni M]] |
| - | [[Category: Villarino, A]] | + | [[Category: Schaeffer F]] |
| - | [[Category: Wehenkel, A]] | + | [[Category: Villarino A]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Wehenkel A]] |
| - | [[Category: Metal binding]]
| + | |
| - | [[Category: Mycobacterium]]
| + | |
| - | [[Category: Pp2c-like phosphatase]]
| + | |
| - | [[Category: Regulatory protein]]
| + | |
| Structural highlights
Function
A0QTQ6_MYCS2
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Phospho-Ser/Thr protein phosphatases (PPs) are dinuclear metalloenzymes classed into two large families, PPP and PPM, on the basis of sequence similarity and metal ion dependence. The archetype of the PPM family is the alpha isoform of human PP2C (PP2Calpha), which folds into an alpha/beta domain similar to those of PPP enzymes. The recent structural studies of three bacterial PPM phosphatases, Mycobacterium tuberculosis MtPstP, Mycobacterium smegmatis MspP, and Streptococcus agalactiae STP, confirmed the conservation of the overall fold and dinuclear metal center in the family, but surprisingly revealed the presence of a third conserved metal-binding site in the active site. To gain insight into the roles of the three-metal center in bacterial enzymes, we report structural and metal-binding studies of MtPstP and MspP. The structure of MtPstP in a new trigonal crystal form revealed a fully active enzyme with the canonical dinuclear metal center but without the third metal ion bound to the catalytic site. The absence of metal correlates with a partially unstructured flap segment, indicating that the third manganese ion contributes to reposition the flap, but is dispensable for catalysis. Studies of metal binding to MspP using isothermal titration calorimetry revealed that the three Mn(2+)-binding sites display distinct affinities, with dissociation constants in the nano- and micromolar range for the two catalytic metal ions and a significantly lower affinity for the third metal-binding site. In agreement, the structure of inactive MspP at acidic pH was determined at atomic resolution and shown to lack the third metal ion in the active site. Structural comparisons of all bacterial phosphatases revealed positional variations in the third metal-binding site that are correlated with the presence of bound substrate and the conformation of the flap segment, supporting a role of this metal ion in assisting enzyme-substrate interactions.
Structural and binding studies of the three-metal center in two mycobacterial PPM Ser/Thr protein phosphatases.,Wehenkel A, Bellinzoni M, Schaeffer F, Villarino A, Alzari PM J Mol Biol. 2007 Dec 7;374(4):890-8. Epub 2007 Oct 2. PMID:17961594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wehenkel A, Bellinzoni M, Schaeffer F, Villarino A, Alzari PM. Structural and binding studies of the three-metal center in two mycobacterial PPM Ser/Thr protein phosphatases. J Mol Biol. 2007 Dec 7;374(4):890-8. Epub 2007 Oct 2. PMID:17961594 doi:http://dx.doi.org/10.1016/j.jmb.2007.09.076
|
