View source for 5nqb


==Rabbit Muscle L-lactate dehydrogenase in complex with malonate==
<StructureSection load='5nqb' size='340' side='right'caption='[[5nqb]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nqb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQB 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]] 1.58&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</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=5nqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqb OCA], [https://pdbe.org/5nqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nqb RCSB], [https://www.ebi.ac.uk/pdbsum/5nqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LDHA_RABIT LDHA_RABIT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metabolites can inhibit the enzymes that generate them. To explore the general nature of metabolic self-inhibition, we surveyed enzymological data accrued from a century of experimentation and generated a genome-scale enzyme-inhibition network. Enzyme inhibition is often driven by essential metabolites, affects the majority of biochemical processes, and is executed by a structured network whose topological organization is reflecting chemical similarities that exist between metabolites. Most inhibitory interactions are competitive, emerge in the close neighbourhood of the inhibited enzymes, and result from structural similarities between substrate and inhibitors. Structural constraints also explain one-third of allosteric inhibitors, a finding rationalized by crystallographic analysis of allosterically inhibited L-lactate dehydrogenase. Our findings suggest that the primary cause of metabolic enzyme inhibition is not the evolution of regulatory metabolite-enzyme interactions, but a finite structural diversity prevalent within the metabolome. In eukaryotes, compartmentalization minimizes inevitable enzyme inhibition and alleviates constraints that self-inhibition places on metabolism.

The self-inhibitory nature of metabolic networks and its alleviation through compartmentalization.,Alam MT, Olin-Sandoval V, Stincone A, Keller MA, Zelezniak A, Luisi BF, Ralser M Nat Commun. 2017 Jul 10;8:16018. doi: 10.1038/ncomms16018. PMID:28691704<ref>PMID:28691704</ref>

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

==See Also==
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Luisi BF]]
[[Category: Olin-Sandoval V]]