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New page: left|200px<br /><applet load="1y8b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y8b" /> '''Solution NMR-Derived Global Fold of Malate S...
 
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[[Image:1y8b.gif|left|200px]]<br /><applet load="1y8b" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution NMR-Derived Global Fold of Malate Synthase G from E.coli'''<br />


==Overview==
==Solution NMR-Derived Global Fold of Malate Synthase G from E.coli==
The size of proteins that can be studied by solution NMR spectroscopy has, increased significantly because of recent developments in methodology., Important experiments include those that make use of approaches that, increase the lifetimes of NMR signals or that define the orientation of, internuclear bond vectors with respect to a common molecular frame. The, advances in NMR techniques are strongly coupled to isotope labeling, methods that increase sensitivity and reduce the complexity of NMR, spectra. We show that these developments can be exploited in structural, studies of high-molecular-weight, single-polypeptide proteins, and we, present the solution global fold of the monomeric 723-residue (82-kDa), enzyme malate synthase G from Escherichia coli, which has been extensively, characterized by NMR in the past several years.
<StructureSection load='1y8b' size='340' side='right'caption='[[1y8b]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1y8b]] 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=1Y8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y8B 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=1y8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8b OCA], [https://pdbe.org/1y8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y8b RCSB], [https://www.ebi.ac.uk/pdbsum/1y8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y8b ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MASZ_ECOLI MASZ_ECOLI] Accounts for almost the entire malate-synthesizing activity in cells metabolizing glyoxylate.[HAMAP-Rule:MF_00641]
== 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/y8/1y8b_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=1y8b ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The size of proteins that can be studied by solution NMR spectroscopy has increased significantly because of recent developments in methodology. Important experiments include those that make use of approaches that increase the lifetimes of NMR signals or that define the orientation of internuclear bond vectors with respect to a common molecular frame. The advances in NMR techniques are strongly coupled to isotope labeling methods that increase sensitivity and reduce the complexity of NMR spectra. We show that these developments can be exploited in structural studies of high-molecular-weight, single-polypeptide proteins, and we present the solution global fold of the monomeric 723-residue (82-kDa) enzyme malate synthase G from Escherichia coli, which has been extensively characterized by NMR in the past several years.


==About this Structure==
Solution NMR-derived global fold of a monomeric 82-kDa enzyme.,Tugarinov V, Choy WY, Orekhov VY, Kay LE Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):622-7. Epub 2005 Jan 6. PMID:15637152<ref>PMID:15637152</ref>
1Y8B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y8B OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution NMR-derived global fold of a monomeric 82-kDa enzyme., Tugarinov V, Choy WY, Orekhov VY, Kay LE, Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):622-7. Epub 2005 Jan 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15637152 15637152]
</div>
<div class="pdbe-citations 1y8b" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Malate synthase 3D structures|Malate synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Malate synthase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Choy W-Y]]
[[Category: Choy, W.Y.]]
[[Category: Kay LE]]
[[Category: Kay, L.E.]]
[[Category: Orekhov VY]]
[[Category: Orekhov, V.Y.]]
[[Category: Tugarinov V]]
[[Category: Tugarinov, V.]]
[[Category: 82 kda enzyme]]
[[Category: apo-malate synthase g]]
[[Category: nmr global fold]]
 
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Latest revision as of 08:01, 15 May 2024

Solution NMR-Derived Global Fold of Malate Synthase G from E.coli

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