2d21
From Proteopedia
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| - | {{Large structure}} | ||
| - | {{STRUCTURE_2d21| PDB=2d21 | SCENE= }} | ||
| - | ===NMR Structure of stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)=== | ||
| - | {{ABSTRACT_PUBMED_16511487}} | ||
| - | == | + | ==NMR Structure of stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)== |
| - | [[2d21]] is a 1 chain structure with sequence from [ | + | <StructureSection load='2d21' size='340' side='right'caption='[[2d21]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2d21]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D21 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=2d21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d21 OCA], [https://pdbe.org/2d21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d21 RCSB], [https://www.ebi.ac.uk/pdbsum/2d21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d21 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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/2d21_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2d21 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nuclear-magnetic-resonance spectroscopy can determine the three-dimensional structure of proteins in solution. However, its potential has been limited by the difficulty of interpreting NMR spectra in the presence of broadened and overlapping resonance lines and low signal-to-noise ratios. Here we present stereo-array isotope labelling (SAIL), a technique that can overcome many of these problems by applying a complete stereospecific and regiospecific pattern of stable isotopes that is optimal with regard to the quality and information content of the resulting NMR spectra. SAIL uses exclusively chemically and enzymatically synthesized amino acids for cell-free protein expression. We demonstrate for the 17-kDa protein calmodulin and the 41-kDa maltodextrin-binding protein that SAIL offers sharpened lines, spectral simplification without loss of information, and the ability to rapidly collect the structural restraints required to solve a high-quality solution structure for proteins twice as large as commonly solved by NMR. It thus makes a large class of proteins newly accessible to detailed solution structure determination. | ||
| - | + | Optimal isotope labelling for NMR protein structure determinations.,Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Guntert P Nature. 2006 Mar 2;440(7080):52-7. PMID:16511487<ref>PMID:16511487</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| + | <div class="pdbe-citations 2d21" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Guntert | + | [[Category: Large Structures]] |
| - | [[Category: Iwashita | + | [[Category: Guntert P]] |
| - | [[Category: Kainosho | + | [[Category: Iwashita Y]] |
| - | [[Category: Ono | + | [[Category: Kainosho M]] |
| - | [[Category: Terauchi | + | [[Category: Ono AM]] |
| - | [[Category: Torizawa | + | [[Category: Terauchi T]] |
| - | + | [[Category: Torizawa T]] | |
| - | + | ||
| - | + | ||
Current revision
NMR Structure of stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP)
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