5y9o: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The ~~entry~~ 5y9o is ~~ON HOLD until Aug 26 2019~~

==The apo structure of Legionella pneumophila WipA==

== Structural highlights ==

<table><tr><td colspan='2'>[[5y9o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y9O FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=5y9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9o OCA], [http://pdbe.org/5y9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y9o RCSB], [http://www.ebi.ac.uk/pdbsum/5y9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9o ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

The gram-negative bacterium Legionella pneumophila invades human's lung and causes Legionnaires' disease. To benefit its survival and replication in cellular milieu, L. pneumophila secrets at least 330 effector proteins into host cells. We found that the effector WipA has the protein tyrosine phosphatase (PTP) activity but does not depend on the classical CX5R motif for activity, suggesting that WipA is an unconventional PTP. Meanwhile, the presence of three other highly conserved motifs typically seen in protein serine/threonine phosphatases and the poor inhibition of WipA activity by okadaic acid led us to propose that WipA is a bacterial protein phosphatase. In addition, the determination of the 2.55-A crystal structure of WipA revealed that WipA resembles cold-active protein tyrosine phosphatase (CAPTPase), and therefore very likely shares the same catalytic mechanism.

~~Authors~~:

Legionella pneumophila effector WipA, a bacterial PPP protein phosphatase with PTP activity.,Jia Q, Lin Y, Gou X, He L, Shen D, Chen D, Xie W, Lu Y Acta Biochim Biophys Sin (Shanghai). 2018 Apr 26. pii: 4986413. doi:, 10.1093/abbs/gmy042. PMID:29701815<ref>PMID:29701815</ref>

~~Description~~:

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

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Jia, Q]]

[[Category: Xie, W]]

[[Category: Peptide binding protein]]

[[Category: Phosphotase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5y9o is ON HOLD  until Aug 26 2019
+==The apo structure of Legionella pneumophila WipA==
+<StructureSection load='5y9o' size='340' side='right' caption='[[5y9o]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5y9o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y9O FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=5y9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9o OCA], [http://pdbe.org/5y9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y9o RCSB], [http://www.ebi.ac.uk/pdbsum/5y9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9o ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The gram-negative bacterium Legionella pneumophila invades human's lung and causes Legionnaires' disease. To benefit its survival and replication in cellular milieu, L. pneumophila secrets at least 330 effector proteins into host cells. We found that the effector WipA has the protein tyrosine phosphatase (PTP) activity but does not depend on the classical CX5R motif for activity, suggesting that WipA is an unconventional PTP. Meanwhile, the presence of three other highly conserved motifs typically seen in protein serine/threonine phosphatases and the poor inhibition of WipA activity by okadaic acid led us to propose that WipA is a bacterial protein phosphatase. In addition, the determination of the 2.55-A crystal structure of WipA revealed that WipA resembles cold-active protein tyrosine phosphatase (CAPTPase), and therefore very likely shares the same catalytic mechanism.
-Authors:
+Legionella pneumophila effector WipA, a bacterial PPP protein phosphatase with PTP activity.,Jia Q, Lin Y, Gou X, He L, Shen D, Chen D, Xie W, Lu Y Acta Biochim Biophys Sin (Shanghai). 2018 Apr 26. pii: 4986413. doi:, 10.1093/abbs/gmy042. PMID:29701815<ref>PMID:29701815</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5y9o" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Jia, Q]]
+[[Category: Xie, W]]
+[[Category: Peptide binding protein]]
+[[Category: Phosphotase]]