1np7: Difference between revisions
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<StructureSection load='1np7' size='340' side='right' caption='[[1np7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1np7' size='340' side='right' caption='[[1np7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1np7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1np7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NP7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1np7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1np7 RCSB], [http://www.ebi.ac.uk/pdbsum/1np7 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=1np7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1np7 OCA], [http://pdbe.org/1np7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1np7 RCSB], [http://www.ebi.ac.uk/pdbsum/1np7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1np7" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Brudler, R]] | [[Category: Brudler, R]] | ||
[[Category: Daiyasu, H]] | [[Category: Daiyasu, H]] | ||
Revision as of 23:29, 10 September 2015
Crystal Structure Analysis of Synechocystis sp. PCC6803 cryptochromeCrystal Structure Analysis of Synechocystis sp. PCC6803 cryptochrome
Structural highlights
Function[CRYD_SYNY3] May have a photoreceptor function. Binds DNA; represses transcription of at least 8 genes, including slr0364 and slr1866. Does not encode a DNA photolyase function. Its disruption does not affect circadian rhythm. 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 PubMedCryptochrome 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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