4prk
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of D-lactate dehydrogenase (D-LDH) from Lactobacillus jensenii== |
| + | <StructureSection load='4prk' size='340' side='right' caption='[[4prk]], [[Resolution|resolution]] 2.13Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4prk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PRK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PRK FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4prl|4prl]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-phosphoerythronate_dehydrogenase 4-phosphoerythronate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.290 1.1.1.290] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4prk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4prk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4prk RCSB], [http://www.ebi.ac.uk/pdbsum/4prk PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The thermostable d-lactate dehydrogenase from Lactobacillus jensenii (Ljd-LDH) is a key enzyme in the production of the d-form of lactic acid from pyruvate concomitant with the oxidation of NADH to NAD(+). The polymers of d-lactic acid are used as biodegradable bioplastics. The crystal structures of Ljd-LDH and in complex with NAD(+) were determined at 2.13 and 2.60A resolutions, respectively. The Ljd-LDH monomer consists of the N-terminal substrate-binding domain and the C-terminal NAD-binding domain. The Ljd-LDH forms a homodimeric structure, and the C-terminal NAD-binding domain mostly enables the dimerization of the enzyme. The NAD cofactor is bound to the GxGxxG NAD-binding motif located between the two domains. Structural comparisons of Ljd-LDH with other d-LDHs reveal that Ljd-LDH has unique amino acid residues at the linker region, which indicates that the open-close dynamics of Ljd-LDH might be different from that of other d-LDHs. Moreover, thermostability experiments showed that the T50(10) value of Ljd-LDH (54.5 degrees C) was much higher than the commercially available d-lactate dehydrogenase (42.7 degrees C). In addition, Ljd-LDH has at least a 7 degrees C higher denaturation temperature compared to commercially available d-LDHs. | ||
| - | + | Crystal structure and thermodynamic properties of d-lactate dehydrogenase from Lactobacillus jensenii.,Kim S, Gu SA, Kim YH, Kim KJ Int J Biol Macromol. 2014 Jul;68:151-7. doi: 10.1016/j.ijbiomac.2014.04.048. Epub, 2014 Apr 30. PMID:24794195<ref>PMID:24794195</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 4-phosphoerythronate dehydrogenase]] | ||
| + | [[Category: Kim, K J.]] | ||
| + | [[Category: Kim, S.]] | ||
| + | [[Category: Nad]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Rossmann fold]] | ||
Revision as of 07:42, 18 June 2014
Crystal structure of D-lactate dehydrogenase (D-LDH) from Lactobacillus jensenii
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