View source for 5xee


==NMR solution structure of the aromatic mutant H43F H67F cytochrome b5==
<StructureSection load='5xee' size='340' side='right'caption='[[5xee]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xee]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XEE FirstGlance]. <br>
</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=5xee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xee OCA], [https://pdbe.org/5xee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xee RCSB], [https://www.ebi.ac.uk/pdbsum/5xee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xee ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYB5_RAT CYB5_RAT] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-6 double bond introduction during the C-6 desaturation.
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== Publication Abstract from PubMed ==
Aromatic interactions are an important force in protein folding as they combine the stability of a hydrophobic interaction with the selectivity of a hydrogen bond. Much of our understanding of aromatic interactions comes from "bioinformatics" based analyses of protein structures and from the contribution of these interactions to stabilizing secondary structure motifs in model peptides. In this study, the structural consequences of aromatic interactions on protein folding have been explored in engineered mutants of the molten globule protein apo-cytochrome b5. Structural changes from disorder to order due to aromatic interactions in two variants of the protein, viz., WF-cytb5 and FF-cytb5, result in significant long-range secondary and tertiary structure. The results show that 54 and 52% of the residues in WF-cytb5 and FF-cytb5, respectively, occupy ordered regions versus 26% in apo-cytochrome b5. The interactions between the aromatic groups are offset-stacked and edge-to-face for the Trp-Phe and Phe-Phe mutants, respectively. Urea denaturation studies indicate that both mutants have a Cm higher than that of apo-cytochrome b5 and are more stable to chaotropic agents than apo-cytochrome b5. The introduction of these aromatic residues also results in "trimer" interactions with existing aromatic groups, reaffirming the selectivity of the aromatic interactions. These studies provide insights into the aromatic interactions that drive disorder-to-order transitions in intrinsically disordered regions of proteins and will aid in de novo protein design beyond small peptide scaffolds.

Engineering Aromatic-Aromatic Interactions To Nucleate Folding in Intrinsically Disordered Regions of Proteins.,Balakrishnan S, Sarma SP Biochemistry. 2017 Aug 22;56(33):4346-4359. doi: 10.1021/acs.biochem.7b00437., Epub 2017 Aug 11. PMID:28738155<ref>PMID:28738155</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5xee" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Balakrishnan S]]
[[Category: Sarma SP]]