View source for 5bmh


==Nitroxide Spin Labels in Protein GB1: T44 Mutant, Crystal Form B==
<StructureSection load='5bmh' size='340' side='right'caption='[[5bmh]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bmh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BMH 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MTN:S-[(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-PYRROL-3-YL)METHYL]+METHANESULFONOTHIOATE'>MTN</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=5bmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bmh OCA], [https://pdbe.org/5bmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bmh RCSB], [https://www.ebi.ac.uk/pdbsum/5bmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bmh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein spin labeling to yield the nitroxide-based R1 side chain is a powerful method to measure protein dynamics and structure by electron spin resonance. However, R1 measurements are complicated by the flexibility of the side chain. While analysis approaches for solvent-exposed alpha-helical environment have been developed to partially account for flexibility, similar work in beta-sheets is lacking. The goal of this study is to provide the first essential steps for understanding the conformational preferences of R1 within edge beta-strands using X-ray crystallography and double electron electron resonance (DEER) distance measurements. Crystal structures yielded seven rotamers for a non-hydrogen-bonded site and three rotamers for a hydrogen-bonded site. The observed rotamers indicate contextual differences in R1 conformational preferences compared to other solvent-exposed environments. For the DEER measurements, each strand site was paired with the same alpha-helical site elsewhere on the protein. The most probable distance observed by DEER is rationalized based on the rotamers observed in the crystal structure. Additionally, the appropriateness of common molecular modeling methods that account for R1 conformational preferences are assessed for the beta-sheet environment. These results show that interpretation of R1 behavior in beta-sheets is difficult and indicate further development is needed for these computational methods to correctly relate DEER distances to protein structure at edge beta-strand sites.

Rotameric preferences of a protein spin label at edge-strand beta-sheet sites.,Cunningham TF, Pornsuwan S, Horne WS, Saxena S Protein Sci. 2016 May;25(5):1049-60. doi: 10.1002/pro.2918. Epub 2016 Mar 21. PMID:26948069<ref>PMID:26948069</ref>

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

==See Also==
*[[Protein G|Protein G]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus sp. 'group G']]
[[Category: Cunningham TC]]
[[Category: Horne WS]]
[[Category: Saxena S]]