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1mkp

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Revision as of 06:52, 25 August 2021

CRYSTAL STRUCTURE OF PYST1 (MKP3)

Structural highlights

1mkp is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DUS6_HUMAN] Inactivates MAP kinases. Has a specificity for the ERK family.

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

The crystal structure of the catalytic domain from the MAPK phosphatase Pyst1 (Pyst1-CD) has been determined at 2.35 A. The structure adopts a protein tyrosine phosphatase (PTPase) fold with a shallow active site that displays a distorted geometry in the absence of its substrate with some similarity to the dual-specificity phosphatase cdc25. Functional characterization of Pyst1-CD indicates it is sufficient to dephosphorylate activated ERK2 in vitro. Kinetic analysis of Pyst1 and Pyst1-CD using the substrate p-nitrophenyl phosphate (pNPP) reveals that both molecules undergo catalytic activation in the presence of recombinant inactive ERK2, switching from a low- to high-activity form. Mutation of Asp 262, located 5.5 A distal to the active site, demonstrates it is essential for catalysis in the high-activity ERK2-dependent conformation of Pyst1 but not for the low-activity ERK2-independent form, suggesting that ERK2 induces closure of the Asp 262 loop over the active site, thereby enhancing Pyst1 catalytic efficiency.

Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation.,Stewart AE, Dowd S, Keyse SM, McDonald NQ Nat Struct Biol. 1999 Feb;6(2):174-81. PMID:10048930^[1]

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

References

↑ Stewart AE, Dowd S, Keyse SM, McDonald NQ. Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation. Nat Struct Biol. 1999 Feb;6(2):174-81. PMID:10048930 doi:10.1038/5861

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mkp"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mkp' size='340' side='right'caption='[[1mkp]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mkp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKP 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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=1mkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkp OCA], [http://pdbe.org/1mkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mkp RCSB], [http://www.ebi.ac.uk/pdbsum/1mkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mkp 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=1mkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkp OCA], [https://pdbe.org/1mkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mkp RCSB], [https://www.ebi.ac.uk/pdbsum/1mkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mkp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DUS6_HUMAN DUS6_HUMAN]] Inactivates MAP kinases. Has a specificity for the ERK family.
+[[https://www.uniprot.org/uniprot/DUS6_HUMAN DUS6_HUMAN]] Inactivates MAP kinases. Has a specificity for the ERK family.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1mkp

From Proteopedia

Revision as of 06:52, 25 August 2021

CRYSTAL STRUCTURE OF PYST1 (MKP3)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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