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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1dld.png|left|200px]]


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==KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE==
The line below this paragraph, containing "STRUCTURE_1dld", creates the "Structure Box" on the page.
<StructureSection load='1dld' size='340' side='right'caption='[[1dld]]' scene=''>
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== Structural highlights ==
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</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>
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{{STRUCTURE_1dld|  PDB=1dld  |  SCENE=  }}
<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===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 7567953 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_7567953}}
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</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLD OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:7567953</ref><references group="xtra"/>
[[Category: Vinals, C]]
[[Category: Vinals, C]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 06:37:54 2010''

Latest revision as of 12:28, 21 July 2021

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTUREKNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Vinals C, De Bolle X, Depiereux E, Feytmans E. Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure. Proteins. 1995 Apr;21(4):307-18. PMID:7567953 doi:http://dx.doi.org/10.1002/prot.340210405
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