View source for 7yqm


==2.9-angstrom cryo-EM structure of Ecoli malate synthase G==
<StructureSection load='7yqm' size='340' side='right'caption='[[7yqm]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH5alpha Escherichia coli DH5alpha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YQM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.89&#8491;</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=7yqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yqm OCA], [https://pdbe.org/7yqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yqm RCSB], [https://www.ebi.ac.uk/pdbsum/7yqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yqm 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]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Determination of sub-100 kDa (kDa) structures by cryo-electron microscopy (EM) is a longstanding but not straightforward goal. Here, we present a 2.9-A cryo-EM structure of a 723-amino acid apo-form malate synthase G (MSG) from Escherichia coli. The cryo-EM structure of the 82-kDa MSG exhibits the same global folding as structures resolved by crystallography and nuclear magnetic resonance (NMR) spectroscopy, and the crystal and cryo-EM structures are indistinguishable. Analyses of MSG dynamics reveal consistent conformational flexibilities among the three experimental approaches, most notably that the alpha/beta domain exhibits structural heterogeneity. We observed that sidechains of F453, L454, M629, and E630 residues involved in hosting the cofactor acetyl-CoA and substrate rotate differently between the cryo-EM apo-form and complex crystal structures. Our work demonstrates that the cryo-EM technique can be used to determine structures and conformational heterogeneity of sub-100 kDa biomolecules to a quality as high as that obtained from X-ray crystallography and NMR spectroscopy.

Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G.,Ho MR, Wu YM, Lu YC, Ko TP, Wu KP J Struct Biol. 2023 Jun;215(2):107958. doi: 10.1016/j.jsb.2023.107958. Epub 2023 , Mar 28. PMID:36997036<ref>PMID:36997036</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yqm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Malate synthase 3D structures|Malate synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lu Y-C]]
[[Category: Wu K-P]]
[[Category: Wu Y-M]]