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3lwt

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Revision as of 03:43, 5 August 2016

Crystal structure of the Yeast Sac1: Implications for its phosphoinositide phosphatase function

Structural highlights

3lwt is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	RSD1, SAC1, YKL212W (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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

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.

Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function.,Manford A, Xia T, Saxena AK, Stefan C, Hu F, Emr SD, Mao Y EMBO J. 2010 May 5;29(9):1489-98. Epub 2010 Apr 13. PMID:20389282^[3]

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

References

↑ Hughes WE, Woscholski R, Cooke FT, Patrick RS, Dove SK, McDonald NQ, Parker PJ. SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases. J Biol Chem. 2000 Jan 14;275(2):801-8. PMID:10625610
↑ Foti M, Audhya A, Emr SD. Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology. Mol Biol Cell. 2001 Aug;12(8):2396-411. PMID:11514624
↑ Manford A, Xia T, Saxena AK, Stefan C, Hu F, Emr SD, Mao Y. Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function. EMBO J. 2010 May 5;29(9):1489-98. Epub 2010 Apr 13. PMID:20389282 doi:10.1038/emboj.2010.57

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lwt"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Yeast Sac1: Implications for its phosphoinositide phosphatase function==
 <StructureSection load='3lwt' size='340' side='right' caption='[[3lwt]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lwt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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>
+<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 Saccharomyces cerevisiae])</td></tr>
+</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://www.rcsb.org/pdb/explore.do?structureId=3lwt RCSB], [http://www.ebi.ac.uk/pdbsum/3lwt PDBsum]</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=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>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lwt ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3lwt" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Phosphoinositide phosphatase|Phosphoinositide phosphatase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Saccharomyces cerevisiae]]
+[[Category: Atcc 18824]]
 [[Category: Emr, S D]]
 [[Category: Hu, F]]

3lwt

From Proteopedia

Revision as of 03:43, 5 August 2016

Crystal structure of the Yeast Sac1: Implications for its phosphoinositide phosphatase function

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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