View source for 4nd5


==Crystal structure of the lactate dehydrogenase from cryptosporidium parvum==
<StructureSection load='4nd5' size='340' side='right'caption='[[4nd5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nd5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporidium_parvum_Iowa_II Cryptosporidium parvum Iowa II]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2frm 2frm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ND5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ND5 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]] 2.1&#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=4nd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nd5 OCA], [https://pdbe.org/4nd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nd5 RCSB], [https://www.ebi.ac.uk/pdbsum/4nd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nd5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5CYZ2_CRYPI Q5CYZ2_CRYPI] 
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== Publication Abstract from PubMed ==
The protozoan parasite Cryptosporidium parvum causes waterborne diseases worldwide. There is no effective therapy for C. parvum infection. The parasite depends mainly on glycolysis for energy production. Lactate dehydrogenase is a major regulator of glycolysis. This paper describes the biochemical characterization of C. parvum lactate dehydrogenase and high resolution crystal structures of the apo-enzyme and four ternary complexes. The ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate. The results reveal distinctive features of the parasitic enzyme. For example, C. parvum lactate dehydrogenase prefers the acetylpyridine analog of NADH as a cofactor. Moreover, it is slightly less sensitive to gossypol inhibition compared with mammalian lactate dehydrogenases and not inhibited by excess pyruvate. The active site loop and the antigenic loop in C. parvum lactate dehydrogenase are considerably different from those in the human counterpart. Structural features and enzymatic properties of C. parvum lactate dehydrogenase are similar to enzymes from related parasites. Structural comparison with malate dehydrogenase supports a common ancestry for the two genes.

Biochemical and structural characterization of Cryptosporidium parvum Lactate dehydrogenase.,Cook WJ, Senkovich O, Hernandez A, Speed H, Chattopadhyay D Int J Biol Macromol. 2015 Mar;74:608-19. doi: 10.1016/j.ijbiomac.2014.12.019., Epub 2014 Dec 24. PMID:25542170<ref>PMID:25542170</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nd5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Cryptosporidium parvum Iowa II]]
[[Category: Large Structures]]
[[Category: Chattopadhyay D]]
[[Category: Cook WJ]]