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PDBsum entry 3mtc
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Hydrolase/hydrolase inhibitor
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PDB id
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3mtc
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase/hydrolase inhibitor
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Title:
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Crystal structure of inpp5b in complex with phosphatidylinositol 4- phosphate
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Structure:
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Type ii inositol-1,4,5-trisphosphate 5-phosphatase. Chain: a. Fragment: unp residues 339-643. Synonym: phosphoinositide 5-phosphatase, 5ptase, 75 kda inositol polyphosphate-5-phosphatase. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: inpp5b. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.40Å
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R-factor:
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0.172
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R-free:
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0.205
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Authors:
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L.Tresaugues,M.Welin,C.H.Arrowsmith,H.Berglund,C.Bountra,R.Collins, A.M.Edwards,S.Flodin,A.Flores,S.Graslund,M.Hammarstrom,I.Johansson, T.Karlberg,S.Kol,T.Kotenyova,M.Moche,T.Nyman,C.Persson,H.Schuler, P.Schutz,M.I.Siponen,A.G.Thorsell,S.Van Der Berg,E.Wahlberg, J.Weigelt,M.Wisniewska,P.Nordlund,Structural Genomics Consortium (Sgc)
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Key ref:
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L.Trésaugues
et al.
(2014).
Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases.
Structure,
22,
744-755.
PubMed id:
DOI:
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Date:
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30-Apr-10
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Release date:
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30-Jun-10
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PROCHECK
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Headers
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References
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P32019
(I5P2_HUMAN) -
Type II inositol 1,4,5-trisphosphate 5-phosphatase from Homo sapiens
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Seq:
Struc:
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993 a.a.
310 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 5 residue positions (black
crosses)
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Enzyme class:
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E.C.3.1.3.36
- phosphoinositide 5-phosphatase.
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Pathway:
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1-Phosphatidyl-myo-inositol Metabolism
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Reaction:
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a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate
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1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate)
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+
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H2O
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=
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1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)
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+
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phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Structure
22:744-755
(2014)
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PubMed id:
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Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases.
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L.Trésaugues,
C.Silvander,
S.Flodin,
M.Welin,
T.Nyman,
S.Gräslund,
M.Hammarström,
H.Berglund,
P.Nordlund.
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ABSTRACT
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SHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase
subfamilies involved in insulin regulation and Lowes syndrome. The structural
basis for membrane recognition, substrate specificity, and regulation of
inositol polyphosphate 5-phophatases is still poorly understood. We determined
the crystal structures of human SHIP2, OCRL, and INPP5B, the latter in complex
with phosphoinositide substrate analogs, which revealed a membrane interaction
patch likely to assist in sequestering substrates from the lipid bilayer.
Residues recognizing the 1-phosphate of the substrates are highly conserved
among human family members, suggesting similar substrate binding modes. However,
3- and 4-phosphate recognition varies and determines individual substrate
specificity profiles. The high conservation of the environment of the scissile
5-phosphate suggests a common reaction geometry for all members of the human
5-phosphatase family.
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Links
