1np7: Difference between revisions

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New page: left|200px<br /><applet load="1np7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1np7, resolution 1.9Å" /> '''Crystal Structure Ana...
 
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[[Image:1np7.jpg|left|200px]]<br /><applet load="1np7" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1np7.jpg|left|200px]]<br /><applet load="1np7" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1np7, resolution 1.9&Aring;" />
caption="1np7, resolution 1.9&Aring;" />
'''Crystal Structure Analysis of Synechocystis sp. PCC6803 cryptochrome'''<br />
'''Crystal Structure Analysis of Synechocystis sp. PCC6803 cryptochrome'''<br />


==Overview==
==Overview==
Cryptochrome flavoproteins, which share sequence homology with, light-dependent DNA repair photolyases, function as photoreceptors in, plants and circadian clock components in animals. Here, we coupled, sequencing of an Arabidopsis cryptochrome gene with phylogenetic, structural, and functional analyses to identify a new cryptochrome class, (cryptochrome DASH) in bacteria and plants, suggesting that cryptochromes, evolved before the divergence of eukaryotes and prokaryotes. The, cryptochrome crystallographic structure, reported here for Synechocystis, cryptochrome DASH, reveals commonalities with photolyases in DNA binding, and redox-dependent function, despite distinct active-site and interaction, surface features. Whole genome transcriptional profiling together with, experimental confirmation of DNA binding indicated that Synechocystis, cryptochrome DASH functions as a transcriptional repressor.
Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene with phylogenetic, structural, and functional analyses to identify a new cryptochrome class (cryptochrome DASH) in bacteria and plants, suggesting that cryptochromes evolved before the divergence of eukaryotes and prokaryotes. The cryptochrome crystallographic structure, reported here for Synechocystis cryptochrome DASH, reveals commonalities with photolyases in DNA binding and redox-dependent function, despite distinct active-site and interaction surface features. Whole genome transcriptional profiling together with experimental confirmation of DNA binding indicated that Synechocystis cryptochrome DASH functions as a transcriptional repressor.


==About this Structure==
==About this Structure==
1NP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with SO4 and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NP7 OCA].  
1NP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP7 OCA].  


==Reference==
==Reference==
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[[Category: Brudler, R.]]
[[Category: Brudler, R.]]
[[Category: Daiyasu, H.]]
[[Category: Daiyasu, H.]]
[[Category: Getzoff, E.D.]]
[[Category: Getzoff, E D.]]
[[Category: Hitomi, K.]]
[[Category: Hitomi, K.]]
[[Category: Ishiura, M.]]
[[Category: Ishiura, M.]]
[[Category: Kanehisa, M.]]
[[Category: Kanehisa, M.]]
[[Category: Kucho, K.]]
[[Category: Kucho, K.]]
[[Category: Roberts, V.A.]]
[[Category: Roberts, V A.]]
[[Category: Tainer, J.A.]]
[[Category: Tainer, J A.]]
[[Category: Todo, T.]]
[[Category: Todo, T.]]
[[Category: Toh, H.]]
[[Category: Toh, H.]]
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[[Category: protein with fad cofactor]]
[[Category: protein with fad cofactor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:27:04 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:37 2008''

Revision as of 15:08, 21 February 2008

File:1np7.jpg


1np7, resolution 1.9Å

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Crystal Structure Analysis of Synechocystis sp. PCC6803 cryptochrome

OverviewOverview

Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene with phylogenetic, structural, and functional analyses to identify a new cryptochrome class (cryptochrome DASH) in bacteria and plants, suggesting that cryptochromes evolved before the divergence of eukaryotes and prokaryotes. The cryptochrome crystallographic structure, reported here for Synechocystis cryptochrome DASH, reveals commonalities with photolyases in DNA binding and redox-dependent function, despite distinct active-site and interaction surface features. Whole genome transcriptional profiling together with experimental confirmation of DNA binding indicated that Synechocystis cryptochrome DASH functions as a transcriptional repressor.

About this StructureAbout this Structure

1NP7 is a Single protein structure of sequence from Synechocystis sp. with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Identification of a new cryptochrome class. Structure, function, and evolution., Brudler R, Hitomi K, Daiyasu H, Toh H, Kucho K, Ishiura M, Kanehisa M, Roberts VA, Todo T, Tainer JA, Getzoff ED, Mol Cell. 2003 Jan;11(1):59-67. PMID:12535521

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