2n45: Difference between revisions

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 ==EC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data with a second set of RDC data simulated for an alternative alignment tensor. Northeast Structural Genomics Consortium target ER690==
-<StructureSection load='2n45' size='340' side='right'caption='[[2n45]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2n45' size='340' side='right'caption='[[2n45]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2n45]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N45 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2n45]] 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=2N45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N45 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mv0|2mv0]], [[1ezp|1ezp]], [[2n42|2n42]], [[2n44|2n44]], [[2n46|2n46]], [[2n47|2n47]], [[2n48|2n48]], [[2n49|2n49]], [[2n4a|2n4a]], [[2n4b|2n4b]], [[2n4c|2n4c]], [[2n4d|2n4d]], [[2n4f|2n4f]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, b4034, JW3994 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=2n45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n45 OCA], [https://pdbe.org/2n45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n45 RCSB], [https://www.ebi.ac.uk/pdbsum/2n45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n45 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
+[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-We have developed an approach for determining NMR structures of proteins over 20 kDa that utilizes sparse distance restraints obtained using transverse relaxation optimized spectroscopy experiments on perdeuterated samples to guide RASREC Rosetta NMR structure calculations. The method was tested on 11 proteins ranging from 15 to 40 kDa, seven of which were previously unsolved. The RASREC Rosetta models were in good agreement with models obtained using traditional NMR methods with larger restraint sets. In five cases X-ray structures were determined or were available, allowing comparison of the accuracy of the Rosetta models and conventional NMR models. In all five cases, the Rosetta models were more similar to the X-ray structures over both the backbone and side-chain conformations than the "best effort" structures determined by conventional methods. The incorporation of sparse distance restraints into RASREC Rosetta allows routine determination of high-quality solution NMR structures for proteins up to 40 kDa, and should be broadly useful in structural biology.
+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.
-Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples.,Lange OF, Rossi P, Sgourakis NG, Song Y, Lee HW, Aramini JM, Ertekin A, Xiao R, Acton TB, Montelione GT, Baker D Proc Natl Acad Sci U S A. 2012 Jul 3;109(27):10873-8. Epub 2012 Jun 25. PMID:22733734<ref>PMID:22733734</ref>
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Hopf, T A]]
+[[Category: Hopf TA]]
-[[Category: Huang, Y J]]
+[[Category: Huang YJ]]
-[[Category: Marks, D]]
+[[Category: Marks D]]
-[[Category: Montelione, G T]]
+[[Category: Montelione GT]]
-[[Category: Structural genomic]]
+[[Category: Sander C]]
-[[Category: Sander, C]]
+[[Category: Tang Y]]
-[[Category: Tang, Y]]
-[[Category: Ec-nmr]]
-[[Category: Nesg]]
-[[Category: Periplasmic binding protein]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Psi-biology]]