6sly: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>
<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLY 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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [https://pdbe.org/6sly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [https://www.ebi.ac.uk/pdbsum/6sly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [https://pdbe.org/6sly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [https://www.ebi.ac.uk/pdbsum/6sly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/TONB_HELPY TONB_HELPY] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).
[https://www.uniprot.org/uniprot/TONB_HELPY TONB_HELPY] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Uniformly (13)C- and (15)N-labeled samples ensure fast and reliable nuclear magnetic resonance (NMR) assignments of proteins and are commonly used for structure elucidation by NMR. However, the preparation of uniformly labeled samples is a labor-intensive and expensive step. Reducing the portion of (13)C-labeled glucose by a factor of five using a fractional 20% (13)C- and 100% (15)N-labeling scheme could lower the total chemical costs, yet retaining sufficient structural information of uniformly [(13)C, (15)N]-labeled sample as a result of the improved sensitivity of NMR instruments. Moreover, fractional (13)C-labeling can facilitate reliable resonance assignments of sidechains because of the biosynthetic pathways of each amino-acid. Preparation of only one [20% (13)C, 100% (15)N]-labeled sample for small proteins (&lt;15 kDa) could also eliminate redundant sample preparations of 100% (15)N-labeled and uniformly 100% [(13)C, (15)N]-labeled samples of proteins. We determined the NMR structures of a small alpha-helical protein, the C domain of IgG-binding protein A from Staphylococcus aureus (SpaC), and a small beta-sheet protein, CBM64 module using [20% (13)C, 100% (15)N]-labeled sample and compared with the crystal structures and the NMR structures derived from the 100% [(13)C, (15)N]-labeled sample. Our results suggest that one [20% (13)C, 100% (15)N]-labeled sample of small proteins could be routinely used as an alternative to conventional 100% [(13)C, (15)N]-labeling for backbone resonance assignments, NMR structure determination, (15)N-relaxation analysis, and ligand-protein interaction.
NMR Structure Determinations of Small Proteins Using only One Fractionally 20% (13)C- and Uniformly 100% (15)N-Labeled Sample.,Heikkinen HA, Backlund SM, Iwai H Molecules. 2021 Feb 1;26(3). pii: molecules26030747. doi:, 10.3390/molecules26030747. PMID:33535444<ref>PMID:33535444</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6sly" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[TonB|TonB]]
*[[TonB|TonB]]
== References ==
<references/>
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