This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2jfr

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:27, 11 July 2018

Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis in complex with phosphate at 0.83 A resolution

Structural highlights

2jfr is a 1 chain structure with sequence from Mycs2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	2jfs, 2jft
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Serine/threonine-specific phosphatases (PPs) represent, after protein tyrosine phosphatases, the second major class of enzymes that catalyze the dephosphorylation of proteins. They are classed in two large families, known as PPP and PPM, on the basis of sequence similarities, metal ion dependence, and inhibitor sensitivity. Despite their wide species distribution and broad physiological roles, the catalytic mechanism of PPM phosphatases has been primarily inferred from studies of a single enzyme, human PP2Calpha. Here, we report the biochemical characterization and the atomic resolution structures of a soluble PPM phosphatase from the saprophyte Mycobacterium smegmatis in complex with different ligands. The structures provide putative snapshots along the catalytic cycle, which support an associative reaction mechanism that differs in some important aspects from the currently accepted model and reinforces the hypothesis of convergent evolution in PPs.

Insights into the catalytic mechanism of PPM Ser/Thr phosphatases from the atomic resolution structures of a mycobacterial enzyme.,Bellinzoni M, Wehenkel A, Shepard W, Alzari PM Structure. 2007 Jul;15(7):863-72. PMID:17637345^[1]

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

References

↑ Bellinzoni M, Wehenkel A, Shepard W, Alzari PM. Insights into the catalytic mechanism of PPM Ser/Thr phosphatases from the atomic resolution structures of a mycobacterial enzyme. Structure. 2007 Jul;15(7):863-72. PMID:17637345 doi:10.1016/j.str.2007.06.002

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jfr"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF THE PPM SER-THR PHOSPHATASE MSPP FROM MYCOBACTERIUM SMEGMATIS IN COMPLEX WITH PHOSPHATE AT 0.83 A RESOLUTION==
+==Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis in complex with phosphate at 0.83 A resolution==
 <StructureSection load='2jfr' size='340' side='right' caption='[[2jfr]], [[Resolution|resolution]] 0.83&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </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>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jfs|2jfs]], [[2jft|2jft]]</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=2jfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfr OCA], [http://pdbe.org/2jfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jfr RCSB], [http://www.ebi.ac.uk/pdbsum/2jfr PDBsum]</span></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=2jfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfr OCA], [http://pdbe.org/2jfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jfr RCSB], [http://www.ebi.ac.uk/pdbsum/2jfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfr ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jf/2jfr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jf/2jfr_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2jfr

From Proteopedia

Revision as of 06:27, 11 July 2018

Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis in complex with phosphate at 0.83 A resolution

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox