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.


7kio

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structure of inositol polyphosphate 1-phosphatase (INPP1) D54A mutant==
==Crystal structure of inositol polyphosphate 1-phosphatase (INPP1) D54A mutant==
-
<StructureSection load='7kio' size='340' side='right'caption='[[7kio]]' scene=''>
+
<StructureSection load='7kio' size='340' side='right'caption='[[7kio]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KIO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7KIO FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7kio]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KIO FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7kio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kio OCA], [http://pdbe.org/7kio PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7kio RCSB], [http://www.ebi.ac.uk/pdbsum/7kio PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7kio ProSAT]</span></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">INPP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Inositol-1,4-bisphosphate_1-phosphatase Inositol-1,4-bisphosphate 1-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.57 3.1.3.57] </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=7kio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kio OCA], [https://pdbe.org/7kio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kio RCSB], [https://www.ebi.ac.uk/pdbsum/7kio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kio ProSAT]</span></td></tr>
</table>
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Inositol polyphosphate 1-phosphatase (INPP1) is a prototype member of metal-dependent/lithium-inhibited phosphomonoesterase protein family defined by a conserved three-dimensional core structure. Enzymes within this family function in distinct pathways including: inositide signaling, gluconeogenesis, and sulfur assimilation. Using structural and biochemical studies, we report the effect of substrate and lithium on a network of metal binding sites within the catalytic center of INPP1. We find that lithium preferentially occupies a key site involved in metal-activation only when substrate or product is added. Mutation of a conserved residue that selectively coordinates the putative lithium-binding site results in a dramatic 100-fold reduction in the inhibitory constant as compared to wild-type. Furthermore, we report the INPP1/inositol 1,4-bisphosphate complex which illuminates key features of the enzyme active site. Our results provide insights into a structural basis for uncompetitive lithium inhibition, substrate recognition and define a sequence motif for metal binding within this family of regulatory phosphatases.
 +
 +
A Structural Basis for Lithium and Substrate Binding of an Inositide Phosphatase.,Dollins DE, Xiong JP, Endo-Streeter S, Anderson DE, Bansal VS, Ponder JW, Ren Y, York JD J Biol Chem. 2020 Nov 10. pii: RA120.014057. doi: 10.1074/jbc.RA120.014057. PMID:33172890<ref>PMID:33172890</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 7kio" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Bovin]]
 +
[[Category: Inositol-1,4-bisphosphate 1-phosphatase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Dollins DE]]
+
[[Category: Dollins, D E]]
-
[[Category: Ren Y]]
+
[[Category: Ren, Y]]
-
[[Category: Xiong J-P]]
+
[[Category: Xiong, J P]]
-
[[Category: York JD]]
+
[[Category: York, J D]]
 +
[[Category: Hydrolase]]

Revision as of 10:09, 14 July 2021

Crystal structure of inositol polyphosphate 1-phosphatase (INPP1) D54A mutant

PDB ID 7kio

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools