1yrx
From Proteopedia
(Difference between revisions)
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<StructureSection load='1yrx' size='340' side='right'caption='[[1yrx]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1yrx' size='340' side='right'caption='[[1yrx]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1yrx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1yrx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides_2.4.1 Cereibacter sphaeroides 2.4.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YRX FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D9G:N-DODECYL-N,N-DIMETHYLGLYCINATE'>D9G</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D9G:N-DODECYL-N,N-DIMETHYLGLYCINATE'>D9G</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yrx OCA], [https://pdbe.org/1yrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yrx RCSB], [https://www.ebi.ac.uk/pdbsum/1yrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yrx ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yrx OCA], [https://pdbe.org/1yrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yrx RCSB], [https://www.ebi.ac.uk/pdbsum/1yrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yrx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q53119_CERSP Q53119_CERSP] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1yrx 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=1yrx ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The flavin-binding BLUF domain of AppA represents a new class of blue light photoreceptors that are present in a number of bacterial and algal species. The dark state X-ray structure of this domain was determined at 2.3 A resolution. The domain demonstrates a new function for the common ferredoxin-like fold; two long alpha-helices flank the flavin, which is bound with its isoalloxazine ring perpendicular to a five-stranded beta-sheet. The hydrogen bond network and the overall protein topology of the BLUF domain (but not its sequence) bear some resemblance to LOV domains, a subset of PAS domains widely involved in signaling. Nearly all residues conserved in BLUF domains surround the flavin chromophore, many of which are involved in an intricate hydrogen bond network. Photoactivation may induce a rearrangement in this network via reorientation of the Gln63 side chain to form a new hydrogen bond to the flavin O4 position. This shift would also break a hydrogen bond to the Trp104 side chain, which may be critical in induction of global structural change in AppA. | ||
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- | Structure of a novel photoreceptor, the BLUF domain of AppA from Rhodobacter sphaeroides.,Anderson S, Dragnea V, Masuda S, Ybe J, Moffat K, Bauer C Biochemistry. 2005 Jun 7;44(22):7998-8005. PMID:15924418<ref>PMID:15924418</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1yrx" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Cereibacter sphaeroides 2 4.1]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Anderson S]] | |
- | [[Category: Anderson | + | [[Category: Bauer C]] |
- | [[Category: Bauer | + | [[Category: Dragnea V]] |
- | [[Category: Dragnea | + | [[Category: Masuda S]] |
- | [[Category: Masuda | + | [[Category: Moffat K]] |
- | [[Category: Moffat | + | [[Category: Ybe J]] |
- | [[Category: Ybe | + | |
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Current revision
Structure of a novel photoreceptor: the BLUF domain of AppA from Rhodobacter sphaeroides
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