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New page: '''Unreleased structure''' The entry 2n48 is ON HOLD Authors: Tang, Y.A. Description: EC-NMR Structure of Escherichia coli YiaD Determined by Combining Evolutionary Couplings (EC) and ... |
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==EC-NMR Structure of Escherichia coli YiaD Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER553== | |||
<StructureSection load='2n48' size='340' side='right'caption='[[2n48]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2n48]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N48 FirstGlance]. <br> | |||
</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=2n48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n48 OCA], [https://pdbe.org/2n48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n48 RCSB], [https://www.ebi.ac.uk/pdbsum/2n48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n48 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/YIAD_ECOLI YIAD_ECOLI] Suppresses temperature-sensitive mutations in BamB when overexpressed. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size. | |||
Protein structure determination by combining sparse NMR data with evolutionary couplings.,Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT Nat Methods. 2015 Jun 29. doi: 10.1038/nmeth.3455. PMID:26121406<ref>PMID:26121406</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Tang | <div class="pdbe-citations 2n48" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Hopf TA]] | |||
[[Category: Huang YJ]] | |||
[[Category: Marks D]] | |||
[[Category: Montelione GT]] | |||
[[Category: Sander C]] | |||
[[Category: Tang Y]] | |||
Latest revision as of 09:14, 15 May 2024
EC-NMR Structure of Escherichia coli YiaD Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER553EC-NMR Structure of Escherichia coli YiaD Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER553
Structural highlights
FunctionYIAD_ECOLI Suppresses temperature-sensitive mutations in BamB when overexpressed. Publication Abstract from PubMedAccurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size. Protein structure determination by combining sparse NMR data with evolutionary couplings.,Tang Y, Huang YJ, Hopf TA, Sander C, Marks DS, Montelione GT Nat Methods. 2015 Jun 29. doi: 10.1038/nmeth.3455. PMID:26121406[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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