4r0o

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'''Unreleased structure'''
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==Crystal structure of PEGylated plastocyanin at 4.2 A resolution==
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<StructureSection load='4r0o' size='340' side='right' caption='[[4r0o]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PLAS_PHOLA PLAS_PHOLA]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4r0o is ON HOLD until Paper Publication
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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>
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Authors: Cattani, G., Vogeley, L., Crowley, P.B.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of PEGylated plastocyanin at 4.2 A resolution
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<div class="pdbe-citations 4r0o" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Crowley, P.B]]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Cattani, G]]
[[Category: Cattani, G]]
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[[Category: Crowley, P B]]
[[Category: Vogeley, L]]
[[Category: Vogeley, L]]
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[[Category: Electron transport]]
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[[Category: Pegylation]]

Revision as of 13:40, 7 October 2015

Crystal structure of PEGylated plastocyanin at 4.2 A resolution

4r0o, resolution 4.20Å

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