3lwt

<StructureSection load='3lwt' size='340' side='right' caption='[[3lwt]], [[Resolution|resolution]] 1.96&Aring;' scene=''>

<table><tr><td colspan='2'>[[3lwt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LWT FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RSD1, SAC1, YKL212W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3lwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lwt OCA], [http://pdbe.org/3lwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lwt RCSB], [http://www.ebi.ac.uk/pdbsum/3lwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lwt ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SAC1_YEAST SAC1_YEAST]] Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton.<ref>PMID:10625610</ref> <ref>PMID:11514624</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lw/3lwt_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Sac family phosphoinositide (PI) phosphatases are an essential family of CX(5)R(T/S)-based enzymes, involved in numerous aspects of cellular function such as PI homeostasis, cellular signalling, and membrane trafficking. Genetic deletions of several Sac family members result in lethality in animal models and mutations of the Sac3 gene have been found in human hereditary diseases. In this study, we report the crystal structure of a founding member of this family, the Sac phosphatase domain of yeast Sac1. The 2.0 A resolution structure shows that the Sac domain comprises of two closely packed sub-domains, a novel N-terminal sub-domain and the PI phosphatase catalytic sub-domain. The structure further shows a striking conformation of the catalytic P-loop and a large positively charged groove at the catalytic site. These findings suggest an unusual mechanism for its dephosphorylation function. Homology structural modeling of human Fig4/Sac3 allows the mapping of several disease-related mutations and provides a framework for the understanding of the molecular mechanisms of human diseases.

 

<div class="pdbe-citations 3lwt" style="background-color:#fffaf0;"></div>

[[Category: Atcc 18824]]

[[Category: Emr, S D]]

[[Category: Hu, F]]

[[Category: Manford, A]]

[[Category: Mao, Y]]

[[Category: Saxena, A K]]

[[Category: Stefan, C]]

[[Category: Xia, T]]

[[Category: Transmembrane]]