4pyh: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4pyh|  PDB=4pyh  |  SCENE=  }}
===Phospho-glucan bound structure of starch phosphatase Starch EXcess4 reveals the mechanism for C6-specificty===


The entry 4pyh is ON HOLD
==Function==
[[http://www.uniprot.org/uniprot/DSP4_ARATH DSP4_ARATH]] Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Acts as major regulator of the initial steps of starch degradation at the granule surface. Functions during the day by dephosphorylating the night-accumulated phospho-oligosaccharides. Can release phosphate from both the C6 and the C3 positions.<ref>PMID:16513634</ref> <ref>PMID:16623901</ref> <ref>PMID:16772378</ref> <ref>PMID:19754155</ref> <ref>PMID:19141707</ref> <ref>PMID:20018599</ref> <ref>PMID:22100529</ref> <ref>PMID:22321580</ref> <ref>PMID:20679247</ref> 


Authors: Meekins, D.A., Vander Kooi, C.W.
==About this Structure==
[[4pyh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PYH OCA].  


Description: Phospho-glucan bound structure of starch phosphatase Starch EXcess4 reveals the mechanism for C6-specificty
==Reference==
<references group="xtra"/><references/>
[[Category: Kooi, C W.Vander.]]
[[Category: Meekins, D A.]]
[[Category: Carbohydrate binding]]
[[Category: Chloroplast]]
[[Category: Dual-specificity phosphatase]]
[[Category: Hydrolase]]
[[Category: Starch phosphatase]]

Revision as of 11:00, 23 April 2014

Template:STRUCTURE 4pyh

Phospho-glucan bound structure of starch phosphatase Starch EXcess4 reveals the mechanism for C6-specifictyPhospho-glucan bound structure of starch phosphatase Starch EXcess4 reveals the mechanism for C6-specificty

FunctionFunction

[DSP4_ARATH] Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Acts as major regulator of the initial steps of starch degradation at the granule surface. Functions during the day by dephosphorylating the night-accumulated phospho-oligosaccharides. Can release phosphate from both the C6 and the C3 positions.[1] [2] [3] [4] [5] [6] [7] [8] [9]

About this StructureAbout this Structure

4pyh is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

  1. ↑ Niittyla T, Comparot-Moss S, Lue WL, Messerli G, Trevisan M, Seymour MD, Gatehouse JA, Villadsen D, Smith SM, Chen J, Zeeman SC, Smith AM. Similar protein phosphatases control starch metabolism in plants and glycogen metabolism in mammals. J Biol Chem. 2006 Apr 28;281(17):11815-8. Epub 2006 Mar 2. PMID:16513634 doi:10.1074/jbc.M600519200
  2. ↑ Kerk D, Conley TR, Rodriguez FA, Tran HT, Nimick M, Muench DG, Moorhead GB. A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch. Plant J. 2006 May;46(3):400-13. PMID:16623901 doi:10.1111/j.1365-313X.2006.02704.x
  3. ↑ Sokolov LN, Dominguez-Solis JR, Allary AL, Buchanan BB, Luan S. A redox-regulated chloroplast protein phosphatase binds to starch diurnally and functions in its accumulation. Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9732-7. Epub 2006 Jun 13. PMID:16772378 doi:10.1073/pnas.0603329103
  4. ↑ Hsu S, Kim Y, Li S, Durrant ES, Pace RM, Woods VL Jr, Gentry MS. Structural insights into glucan phosphatase dynamics using amide hydrogen-deuterium exchange mass spectrometry. Biochemistry. 2009 Oct 20;48(41):9891-902. doi: 10.1021/bi9008853. PMID:19754155 doi:10.1021/bi9008853
  5. ↑ Kotting O, Santelia D, Edner C, Eicke S, Marthaler T, Gentry MS, Comparot-Moss S, Chen J, Smith AM, Steup M, Ritte G, Zeeman SC. STARCH-EXCESS4 is a laforin-like Phosphoglucan phosphatase required for starch degradation in Arabidopsis thaliana. Plant Cell. 2009 Jan;21(1):334-46. doi: 10.1105/tpc.108.064360. Epub 2009 Jan 13. PMID:19141707 doi:10.1105/tpc.108.064360
  6. ↑ Hejazi M, Fettke J, Kotting O, Zeeman SC, Steup M. The Laforin-like dual-specificity phosphatase SEX4 from Arabidopsis hydrolyzes both C6- and C3-phosphate esters introduced by starch-related dikinases and thereby affects phase transition of alpha-glucans. Plant Physiol. 2010 Feb;152(2):711-22. doi: 10.1104/pp.109.149914. Epub 2009 Dec , 16. PMID:20018599 doi:10.1104/pp.109.149914
  7. ↑ Santelia D, Kotting O, Seung D, Schubert M, Thalmann M, Bischof S, Meekins DA, Lutz A, Patron N, Gentry MS, Allain FH, Zeeman SC. The phosphoglucan phosphatase like sex Four2 dephosphorylates starch at the C3-position in Arabidopsis. Plant Cell. 2011 Nov;23(11):4096-111. doi: 10.1105/tpc.111.092155. Epub 2011 Nov , 18. PMID:22100529 doi:10.1105/tpc.111.092155
  8. ↑ Weise SE, Aung K, Jarou ZJ, Mehrshahi P, Li Z, Hardy AC, Carr DJ, Sharkey TD. Engineering starch accumulation by manipulation of phosphate metabolism of starch. Plant Biotechnol J. 2012 Jun;10(5):545-54. doi: 10.1111/j.1467-7652.2012.00684.x., Epub 2012 Feb 9. PMID:22321580 doi:10.1111/j.1467-7652.2012.00684.x
  9. ↑ Vander Kooi CW, Taylor AO, Pace RM, Meekins DA, Guo HF, Kim Y, Gentry MS. Structural basis for the glucan phosphatase activity of Starch Excess4. Proc Natl Acad Sci U S A. 2010 Aug 31;107(35):15379-84. Epub 2010 Aug 2. PMID:20679247 doi:10.1073/pnas.1009386107

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