7sws: Difference between revisions

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<StructureSection load='7sws' size='340' side='right'caption='[[7sws]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
<StructureSection load='7sws' size='340' side='right'caption='[[7sws]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7sws]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Acropora_millepora Acropora millepora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SWS FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SWS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.642&#8491;</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]] 1.642&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</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=7sws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sws OCA], [https://pdbe.org/7sws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sws RCSB], [https://www.ebi.ac.uk/pdbsum/7sws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sws 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=7sws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sws OCA], [https://pdbe.org/7sws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sws RCSB], [https://www.ebi.ac.uk/pdbsum/7sws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sws ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q66PV0_ACRMI Q66PV0_ACRMI]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Anthozoan chromoproteins are highly pigmented, diversely coloured and readily produced in recombinant expression systems. While they are a versatile and powerful building block in synthetic biology for applications such as biosensor development, they are not widely used in comparison to the related fluorescent proteins, partly due to a lack of structural characterization to aid protein engineering. Here, high-resolution X-ray crystal structures of four open-source chromoproteins, gfasPurple, amilCP, spisPink and eforRed, are presented. These proteins are dimers in solution, and mutation at the conserved dimer interface leads to loss of visible colour development in gfasPurple. The chromophores are trans and noncoplanar in gfasPurple, amilCP and spisPink, while that in eforRed is cis and noncoplanar, and also emits fluorescence. Like other characterized chromoproteins, gfasPurple, amilCP and eforRed contain an sp(2)-hybridized N-acylimine in the peptide bond preceding the chromophore, while spisPink is unusual and demonstrates a true sp(3)-hybridized trans-peptide bond at this position. It was found that point mutations at the chromophore-binding site in gfasPurple that substitute similar amino acids to those in amilCP and spisPink generate similar colours. These features and observations have implications for the utility of these chromoproteins in protein engineering and synthetic biology applications.
Over the rainbow: structural characterization of the chromoproteins gfasPurple, amilCP, spisPink and eforRed.,Ahmed FH, Caputo AT, French NG, Peat TS, Whitfield J, Warden AC, Newman J, Scott C Acta Crystallogr D Struct Biol. 2022 May 1;78(Pt 5):599-612. doi:, 10.1107/S2059798322002625. Epub 2022 Apr 8. PMID:35503208<ref>PMID:35503208</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sws" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acropora millepora]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ahmed H]]
[[Category: Ahmed H]]

Latest revision as of 12:35, 9 October 2024

Crystal structure of the chromoprotein amilCPCrystal structure of the chromoprotein amilCP

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.642Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

7sws, resolution 1.64Å

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