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[[ | ==KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE== | ||
<StructureSection load='1dld' size='340' side='right'caption='[[1dld]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLD FirstGlance]. <br> | |||
</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=1dld FirstGlance], [https://www.ebi.ac.uk/pdbsum/1dld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dld ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A three-dimensional structure of the NAD-dependent D-lactate dehydrogenase of Lactobacillus bulgaricus is modeled using the structure of the formate dehydrogenase of Pseudomonas sp. as template. Both sequences share only 22% of identical residues. Regions for knowledge-based modeling are defined from the structurally conserved regions predicted by multiple alignment of a set of related protein sequences with low homology. The model of the D-LDH subunit shows, as for the formate dehydrogenase, an alpha/beta structure, with a catalytic domain and a coenzyme binding domain. It points out the catalytic histidine (His-296) and supports the hypothetical catalytic mechanism. It also suggests that the other residues involved in the active site are Arg-235, possibly involved in the binding of the carboxyl group of the pyruvate, and Phe-299, a candidate for stabilizing the methyl group of the substrate. | |||
Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure.,Vinals C, De Bolle X, Depiereux E, Feytmans E Proteins. 1995 Apr;21(4):307-18. PMID:7567953<ref>PMID:7567953</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1dld" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Vinals, C]] | [[Category: Vinals, C]] | ||
Latest revision as of 12:28, 21 July 2021
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KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTUREKNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE
Structural highlights
Publication Abstract from PubMedA three-dimensional structure of the NAD-dependent D-lactate dehydrogenase of Lactobacillus bulgaricus is modeled using the structure of the formate dehydrogenase of Pseudomonas sp. as template. Both sequences share only 22% of identical residues. Regions for knowledge-based modeling are defined from the structurally conserved regions predicted by multiple alignment of a set of related protein sequences with low homology. The model of the D-LDH subunit shows, as for the formate dehydrogenase, an alpha/beta structure, with a catalytic domain and a coenzyme binding domain. It points out the catalytic histidine (His-296) and supports the hypothetical catalytic mechanism. It also suggests that the other residues involved in the active site are Arg-235, possibly involved in the binding of the carboxyl group of the pyruvate, and Phe-299, a candidate for stabilizing the methyl group of the substrate. Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure.,Vinals C, De Bolle X, Depiereux E, Feytmans E Proteins. 1995 Apr;21(4):307-18. PMID:7567953[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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