4nd3: Difference between revisions
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==Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (l-lactic acid) and cofactor (b-nicotinamide adenine dinucleotide)== | ==Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (l-lactic acid) and cofactor (b-nicotinamide adenine dinucleotide)== | ||
<StructureSection load='4nd3' size='340' side='right' caption='[[4nd3]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='4nd3' size='340' side='right'caption='[[4nd3]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nd3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ND3 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4nd3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporidium_parvum_Iowa_II Cryptosporidium parvum Iowa II]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ND3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ND3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=4nd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nd3 OCA], [https://pdbe.org/4nd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nd3 RCSB], [https://www.ebi.ac.uk/pdbsum/4nd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nd3 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5CYZ2_CRYPI Q5CYZ2_CRYPI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4nd3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4nd3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cryptosporidium parvum Iowa II]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chattopadhyay D]] | ||
[[Category: | [[Category: Cook WJ]] | ||
Latest revision as of 19:54, 20 September 2023
Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (l-lactic acid) and cofactor (b-nicotinamide adenine dinucleotide)Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (l-lactic acid) and cofactor (b-nicotinamide adenine dinucleotide)
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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