View source for 3wsv


==Crystal structure of minor L-lactate dehydrogenase from Enterococcus mundtii in the ligands-unbound form==
<StructureSection load='3wsv' size='340' side='right'caption='[[3wsv]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wsv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_mundtii Enterococcus mundtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSV 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]] 2.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3wsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsv OCA], [https://pdbe.org/3wsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wsv RCSB], [https://www.ebi.ac.uk/pdbsum/3wsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wsv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/V5XPB8_ENTMU V5XPB8_ENTMU] Catalyzes the conversion of lactate to pyruvate.[HAMAP-Rule:MF_00488]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A plant-derived Enterococcus mundtii 15-1A, that has been previously isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia by our group, possesses two kinds of l-lactate dehydrogenase (l-LDH): LDH-1 and LDH-2. LDH-1 was activated under low concentration of fluctose-1,6-bisphosphate (FBP) at both pH 5.5 and 7.5. Although LDH-2 was also activated under the low concentration of FBP at pH 5.5, a high concentration of FBP is necessary to activate it at pH 7.5. The present study shows the crystal structures of the acidophilic LDH-2 in a complex with and without FBP and NADH. Although the tertiary structure of the ligands-bound LDH-2 is similar to that of the active form of other bacterial l-LDHs, the structure without the ligands is different from that of any other previously determined l-LDHs. Major structural alterations between the two structures of LDH-2 were observed at two regions in one subunit. At the N-terminal parts of the two regions, the ligands-bound form takes an alpha-helical structure, while the form without ligands displays more disordered and extended structures. A vacuum-ultraviolet circular dichroism analysis showed that the alpha-helix content of LDH-2 in solution is approximately 30% at pH 7.5, which is close to that in the crystal structure of the form without ligands. A D241N mutant of LDH-2, which was created by us to easily form an alpha-helix at one of the two parts, exhibited catalytic activity even in the absence of FBP at both pH 5.5 and 7.5.

An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A.,Matoba Y, Miyasako M, Matsuo K, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M FEBS Open Bio. 2014 Sep 6;4:834-47. doi: 10.1016/j.fob.2014.08.006. eCollection, 2014. PMID:25379380<ref>PMID:25379380</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wsv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterococcus mundtii]]
[[Category: Large Structures]]
[[Category: Matoba Y]]
[[Category: Sugiyama M]]