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.

4nyh

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 13:02, 5 August 2016

Orthorhombic crystal form of pir1 dual specificity phosphatase core

Structural highlights

4nyh is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4mbb
Gene:	DUSP11, PIR1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DUS11_HUMAN] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.^[1]

Publication Abstract from PubMed

PIR1 is an atypical dual-specificity phosphatase (DSP) that dephosphorylates RNA with a higher specificity than phosphoproteins. Here we report the atomic structure of a catalytically inactive mutant (C152S) of the human PIR1 phosphatase core (PIR1-core, residues 29-205), refined at 1.20 A resolution. PIR1-core shares structural similarities with DSPs related to Vaccinia virus VH1 and with RNA 5'-phosphatases such as the baculovirus RNA triphosphatase and the human mRNA capping enzyme. The PIR1 active site cleft is wider and deeper than that of VH1 and contains two bound ions: a phosphate trapped above the catalytic cysteine C152 exemplifies the binding mode expected for the gamma-phosphate of RNA, and approximately 6 A away, a chloride ion coordinates the general base R158. Two residues in the PIR1 phosphate-binding loop (P-loop), a histidine (H154) downstream of C152 and an asparagine (N157) preceding R158, make close contacts with the active site phosphate, and their nonaliphatic side chains are essential for phosphatase activity in vitro. These residues are conserved in all RNA 5'-phosphatases that, analogous to PIR1, lack a "general acid" residue. Thus, a deep active site crevice, two active site ions, and conserved P-loop residues stabilizing the gamma-phosphate of RNA are defining features of atypical DSPs that specialize in dephosphorylating 5'-RNA.

Structure of Human PIR1, an Atypical Dual-Specificity Phosphatase.,Sankhala RS, Lokareddy RK, Cingolani G Biochemistry. 2014 Feb 11;53(5):862-71. doi: 10.1021/bi401240x. Epub 2014 Jan 31. PMID:24447265^[2]

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

References

↑ Yuan Y, Li DM, Sun H. PIR1, a novel phosphatase that exhibits high affinity to RNA . ribonucleoprotein complexes. J Biol Chem. 1998 Aug 7;273(32):20347-53. PMID:9685386
↑ Sankhala RS, Lokareddy RK, Cingolani G. Structure of Human PIR1, an Atypical Dual-Specificity Phosphatase. Biochemistry. 2014 Feb 11;53(5):862-71. doi: 10.1021/bi401240x. Epub 2014 Jan 31. PMID:24447265 doi:http://dx.doi.org/10.1021/bi401240x

1 Structural highlights
2 Function
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/4nyh"

@@ Line 1: / Line 1: @@
 ==Orthorhombic crystal form of pir1 dual specificity phosphatase core==
 <StructureSection load='4nyh' size='340' side='right' caption='[[4nyh]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mbb|4mbb]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DUSP11, PIR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [http://www.ebi.ac.uk/pdbsum/4nyh 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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [http://pdbe.org/4nyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [http://www.ebi.ac.uk/pdbsum/4nyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyh ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4nyh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4nyh

From Proteopedia

Revision as of 13:02, 5 August 2016

Orthorhombic crystal form of pir1 dual specificity phosphatase core

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox