4r0o: Difference between revisions
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''' | ==Crystal structure of PEGylated plastocyanin at 4.2 A resolution== | ||
<StructureSection load='4r0o' size='340' side='right' caption='[[4r0o]], [[Resolution|resolution]] 4.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4r0o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R0O FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=LCY:1-METHYLPYRROLIDINE-2,5-DIONE'>LCY</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=4r0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0o OCA], [http://pdbe.org/4r0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r0o RCSB], [http://www.ebi.ac.uk/pdbsum/4r0o PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PLAS_PHOLA PLAS_PHOLA]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
PEGylated proteins are a mainstay of the biopharmaceutical industry. Although the use of poly(ethylene glycol) (PEG) to increase particle size, stability and solubility is well-established, questions remain as to the structure of PEG-protein conjugates. Here we report the structural characterization of a model beta-sheet protein (plastocyanin, 11.5 kDa) modified with a single PEG 5,000. An NMR spectroscopy study of the PEGylated conjugate indicated that the protein and PEG behaved as independent domains. A crystal structure revealed an extraordinary double-helical assembly of the conjugate, with the helices arranged orthogonally to yield a highly porous architecture. Electron density was not observed for the PEG chain, which indicates that it was disordered. The volume available per PEG chain in the crystal was within 10% of the calculated random coil volume. Together, these data support a minimal interaction between the protein and the synthetic polymer. Our work provides new possibilities for understanding this important class of protein-polymer hybrids and suggests a novel approach to engineering protein assemblies. | |||
Structure of a PEGylated protein reveals a highly porous double-helical assembly.,Cattani G, Vogeley L, Crowley PB Nat Chem. 2015 Oct;7(10):823-8. doi: 10.1038/nchem.2342. Epub 2015 Sep 7. PMID:26391082<ref>PMID:26391082</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4r0o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cattani, G]] | [[Category: Cattani, G]] | ||
[[Category: Crowley, P B]] | |||
[[Category: Vogeley, L]] | [[Category: Vogeley, L]] | ||
[[Category: Electron transport]] | |||
[[Category: Pegylation]] | |||
Revision as of 13:40, 7 October 2015
Crystal structure of PEGylated plastocyanin at 4.2 A resolution
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