View source for 5ulv


==Malate dehydrogenase from Methylobacterium extorquens==
<StructureSection load='5ulv' size='340' side='right'caption='[[5ulv]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ulv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens Methylorubrum extorquens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ror 4ror]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ULV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ULV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5ulv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ulv OCA], [https://pdbe.org/5ulv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ulv RCSB], [https://www.ebi.ac.uk/pdbsum/5ulv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ulv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MDH_METEA MDH_METEA] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Three high-resolution X-ray crystal structures of malate dehydrogenase (MDH; EC 1.1.1.37) from the methylotroph Methylobacterium extorquens AM1 are presented. By comparing the structures of apo MDH, a binary complex of MDH and NAD(+), and a ternary complex of MDH and oxaloacetate with ADP-ribose occupying the pyridine nucleotide-binding site, conformational changes associated with the formation of the catalytic complex were characterized. While the substrate-binding site is accessible in the enzyme resting state or NAD(+)-bound forms, the substrate-bound form exhibits a closed conformation. This conformational change involves the transition of an alpha-helix to a 310-helix, which causes the adjacent loop to close the active site following coenzyme and substrate binding. In the ternary complex, His284 forms a hydrogen bond to the C2 carbonyl of oxaloacetate, placing it in a position to donate a proton in the formation of (2S)-malate.

Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase.,Gonzalez JM, Marti-Arbona R, Chen JCH, Broom-Peltz B, Unkefer CJ Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):610-616. doi:, 10.1107/S2053230X18011809. Epub 2018 Sep 19. PMID:30279311<ref>PMID:30279311</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ulv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylorubrum extorquens]]
[[Category: Gonzalez JM]]