6e3b: Difference between revisions
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==STRUCTURE OF Siw14 CATALYTIC CORE== | |||
<StructureSection load='6e3b' size='340' side='right' caption='[[6e3b]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6e3b]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E3B FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q47|2q47]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=6e3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e3b OCA], [http://pdbe.org/6e3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e3b RCSB], [http://www.ebi.ac.uk/pdbsum/6e3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e3b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SIW14_YEAST SIW14_YEAST]] Plays a role in actin filament organization and endocytosis.<ref>PMID:15020461</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Siw14 is a recently discovered inositol phosphatase implicated in suppressing prion propagation in Saccharomyces cerevisiae. In this paper, we used hybrid structural methods to decipher Siw14 molecular architecture. We found the protein exists in solution as an elongated monomer that is approximately 140 A in length, containing an acidic N-terminal domain and a basic C-terminal dual-specificity phosphatase (DSP) domain, structurally similar to the glycogen phosphatase laforin. The two domains are connected by a protease susceptible linker and do not interact in vitro. The crystal structure of Siw14-DSP reveals a highly basic phosphate-binding loop and an approximately 10 A deep substrate-binding crevice that evolved to dephosphorylate pyro-phosphate moieties. A pseudoatomic model of the full-length phosphatase generated from solution, crystallographic, biochemical, and modeling data sheds light on the interesting zwitterionic nature of Siw14, which we hypothesized may play a role in discriminating negatively charged inositol phosphates. | |||
Molecular Architecture of the Inositol Phosphatase Siw14.,Florio TJ, Lokareddy RK, Gillilan RE, Cingolani G Biochemistry. 2019 Feb 12;58(6):534-545. doi: 10.1021/acs.biochem.8b01044. Epub, 2019 Jan 3. PMID:30548067<ref>PMID:30548067</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6e3b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Protein-tyrosine-phosphatase]] | |||
[[Category: Cingolani, G]] | [[Category: Cingolani, G]] | ||
[[Category: Florio, T]] | [[Category: Florio, T]] | ||
[[Category: Lokareddy, R]] | [[Category: Lokareddy, R]] | ||
[[Category: Dual specificity phosphatase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Inositol phosphate]] | |||
[[Category: Vh1-like phosphatase]] | |||
Revision as of 18:17, 27 February 2019
STRUCTURE OF Siw14 CATALYTIC CORESTRUCTURE OF Siw14 CATALYTIC CORE
Structural highlights
Function[SIW14_YEAST] Plays a role in actin filament organization and endocytosis.[1] Publication Abstract from PubMedSiw14 is a recently discovered inositol phosphatase implicated in suppressing prion propagation in Saccharomyces cerevisiae. In this paper, we used hybrid structural methods to decipher Siw14 molecular architecture. We found the protein exists in solution as an elongated monomer that is approximately 140 A in length, containing an acidic N-terminal domain and a basic C-terminal dual-specificity phosphatase (DSP) domain, structurally similar to the glycogen phosphatase laforin. The two domains are connected by a protease susceptible linker and do not interact in vitro. The crystal structure of Siw14-DSP reveals a highly basic phosphate-binding loop and an approximately 10 A deep substrate-binding crevice that evolved to dephosphorylate pyro-phosphate moieties. A pseudoatomic model of the full-length phosphatase generated from solution, crystallographic, biochemical, and modeling data sheds light on the interesting zwitterionic nature of Siw14, which we hypothesized may play a role in discriminating negatively charged inositol phosphates. Molecular Architecture of the Inositol Phosphatase Siw14.,Florio TJ, Lokareddy RK, Gillilan RE, Cingolani G Biochemistry. 2019 Feb 12;58(6):534-545. doi: 10.1021/acs.biochem.8b01044. Epub, 2019 Jan 3. PMID:30548067[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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