1i9y

From Proteopedia

(Difference between revisions)

Revision as of 07:38, 7 April 2021

CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN

Structural highlights

1i9y is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1i9z
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SYJ1_SCHPO] Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Involved in distinct membrane trafficking and signal transduction pathways. Highly active against a range of soluble and lipid inositol phosphates. Active in dephosphorylating the 5-position of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented in sonicated vesicles and Triton mixed micelles, and somewhat less active against PI(3,5)P2 in unilamellar vesicles. Activity against PI(3,5)P2 drops sharply when this substrate is presented in mixed micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2.^[1]

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

Inositol polyphosphate 5-phosphatases are central to intracellular processes ranging from membrane trafficking to Ca(2+) signaling, and defects in this activity result in the human disease Lowe syndrome. The 1.8 resolution structure of the inositol polyphosphate 5-phosphatase domain of SPsynaptojanin bound to Ca(2+) and inositol (1,4)-bisphosphate reveals a fold and an active site His and Asp pair resembling those of several Mg(2+)-dependent nucleases. Additional loops mediate specific inositol polyphosphate contacts. The 4-phosphate of inositol (1,4)-bisphosphate is misoriented by 4.6 compared to the reactive geometry observed in the apurinic/apyrimidinic endonuclease 1, explaining the dephosphorylation site selectivity of the 5-phosphatases. Based on the structure, a series of mutants are described that exhibit altered substrate specificity providing general determinants for substrate recognition.

Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase.,Tsujishita Y, Guo S, Stolz LE, York JD, Hurley JH Cell. 2001 May 4;105(3):379-89. PMID:11348594^[2]

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

References

↑ Chi Y, Zhou B, Wang WQ, Chung SK, Kwon YU, Ahn YH, Chang YT, Tsujishita Y, Hurley JH, Zhang ZY. Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2. J Biol Chem. 2004 Oct 22;279(43):44987-95. Epub 2004 Aug 16. PMID:15316017 doi:http://dx.doi.org/10.1074/jbc.M406416200
↑ Tsujishita Y, Guo S, Stolz LE, York JD, Hurley JH. Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase. Cell. 2001 May 4;105(3):379-89. PMID:11348594

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i9y"

@@ Line 3: / Line 3: @@
 <StructureSection load='1i9y' size='340' side='right'caption='[[1i9y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1i9y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1i9y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9Y FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i9z|1i9z]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i9z|1i9z]]</div></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=1i9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9y OCA], [http://pdbe.org/1i9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i9y RCSB], [http://www.ebi.ac.uk/pdbsum/1i9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9y 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=1i9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9y OCA], [https://pdbe.org/1i9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9y RCSB], [https://www.ebi.ac.uk/pdbsum/1i9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SYJ1_SCHPO SYJ1_SCHPO]] Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Involved in distinct membrane trafficking and signal transduction pathways. Highly active against a range of soluble and lipid inositol phosphates. Active in dephosphorylating the 5-position of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented in sonicated vesicles and Triton mixed micelles, and somewhat less active against PI(3,5)P2 in unilamellar vesicles. Activity against PI(3,5)P2 drops sharply when this substrate is presented in mixed micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2.<ref>PMID:15316017</ref>
+[[https://www.uniprot.org/uniprot/SYJ1_SCHPO SYJ1_SCHPO]] Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Involved in distinct membrane trafficking and signal transduction pathways. Highly active against a range of soluble and lipid inositol phosphates. Active in dephosphorylating the 5-position of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 and to a lesser extent Ins(1,4,5,6)P4. The enzyme is also active against PI(4,5)P2 presented in sonicated vesicles and Triton mixed micelles, and somewhat less active against PI(3,5)P2 in unilamellar vesicles. Activity against PI(3,5)P2 drops sharply when this substrate is presented in mixed micelles. Also hydrolyzes PIP3 to produce PI(3,4)P2.<ref>PMID:15316017</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1i9y

From Proteopedia

Revision as of 07:38, 7 April 2021

CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox