1y6i: Difference between revisions
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'''Synechocystis GUN4''' | {{Structure | ||
|PDB= 1y6i |SIZE=350|CAPTION= <scene name='initialview01'>1y6i</scene>, resolution 1.78Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= gun4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]) | |||
}} | |||
'''Synechocystis GUN4''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Y6I is a [ | 1Y6I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6I OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the Mg-chelatase cofactor GUN4 reveals a novel hand-shaped fold for porphyrin binding., Verdecia MA, Larkin RM, Ferrer JL, Riek R, Chory J, Noel JP, PLoS Biol. 2005 May;3(5):e151. Epub 2005 Apr 26. PMID:[http:// | Structure of the Mg-chelatase cofactor GUN4 reveals a novel hand-shaped fold for porphyrin binding., Verdecia MA, Larkin RM, Ferrer JL, Riek R, Chory J, Noel JP, PLoS Biol. 2005 May;3(5):e151. Epub 2005 Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15884974 15884974] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
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[[Category: porphyrin binding]] | [[Category: porphyrin binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:18:58 2008'' | ||
Revision as of 13:18, 20 March 2008
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| 1y6i, resolution 1.78Å | |||||||||||||
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| Gene: | gun4 (Synechocystis sp.) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Synechocystis GUN4
Overview
In plants, the accumulation of the chlorophyll precursor Mg-protoporphyrin IX (Mg-Proto) in the plastid regulates the expression of a number of nuclear genes with functions related to photosynthesis. Analysis of the plastid-to-nucleus signaling activity of Mg-Proto in Arabidopsis thaliana led to the discovery of GUN4, a novel porphyrin-binding protein that also dramatically enhances the activity of Mg-chelatase, the enzyme that synthesizes Mg-Proto. GUN4 may also play a role in both photoprotection and the cellular shuttling of tetrapyrroles. Here we report a 1.78-A resolution crystal structure of Synechocystis GUN4, in which the porphyrin-binding domain adopts a unique three dimensional fold with a "cupped hand" shape. Biophysical and biochemical analyses revealed the specific site of interaction between GUN4 and Mg-Proto and the energetic determinants for the GUN4.Mg-Proto interaction. Our data support a novel protective function for GUN4 in tetrapyrrole trafficking. The combined structural and energetic analyses presented herein form the physical-chemical basis for understanding GUN4 biological activity, including its role in the stimulation of Mg-chelatase activity, as well as in Mg-Proto retrograde signaling.
About this Structure
1Y6I is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
Structure of the Mg-chelatase cofactor GUN4 reveals a novel hand-shaped fold for porphyrin binding., Verdecia MA, Larkin RM, Ferrer JL, Riek R, Chory J, Noel JP, PLoS Biol. 2005 May;3(5):e151. Epub 2005 Apr 26. PMID:15884974
Page seeded by OCA on Thu Mar 20 15:18:58 2008
