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[[Image:1j49.gif|left|200px]]
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{{STRUCTURE_1j49|  PDB=1j49  |  SCENE=  }}
'''INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS'''


==INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS==
<StructureSection load='1j49' size='340' side='right'caption='[[1j49]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1j49]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_delbrueckii_subsp._bulgaricus Lactobacillus delbrueckii subsp. bulgaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J49 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1j49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j49 OCA], [https://pdbe.org/1j49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j49 RCSB], [https://www.ebi.ac.uk/pdbsum/1j49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j49 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LDHD_LACDA LDHD_LACDA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j4/1j49_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j49 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
NAD-dependent Lactobacillus bulgaricus D-Lactate dehydrogenase (D-LDHb) catalyses the reversible conversion of pyruvate into D-lactate. Crystals of D-LDHb complexed with NADH were grown and X-ray data collected to 2.2 A. The structure of D-LDHb was solved by molecular replacement using the dimeric Lactobacillus helveticus D-LDH as a model and was refined to an R-factor of 20.7%. The two subunits of the enzyme display strong asymmetry due to different crystal environments. The opening angles of the two catalytic domains with respect to the core coenzyme binding domains differ by 16 degrees. Subunit A is in an "open" conformation typical for a dehydrogenase apo enzyme and subunit B is "closed". The NADH-binding site in subunit A is only 30% occupied, while in subunit B it is fully occupied and there is a sulphate ion in the substrate-binding pocket. A pyruvate molecule has been modelled in the active site and its orientation is in agreement with existing kinetic and structural data. On domain closure, a cluster of hydrophobic residues packs tightly around the methyl group of the modelled pyruvate molecule. At least three residues from this cluster govern the substrate specificity. Substrate binding itself contributes to the stabilisation of domain closure and activation of the enzyme. In pyruvate reduction, D-LDH can adapt another protonated residue, a lysine residue, to accomplish the role of the acid catalyst His296. Required lowering of the lysine pK(a) value is explained on the basis of the H296K mutant structure.


==Overview==
Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.,Razeto A, Kochhar S, Hottinger H, Dauter M, Wilson KS, Lamzin VS J Mol Biol. 2002 Apr 19;318(1):109-19. PMID:12054772<ref>PMID:12054772</ref>
NAD-dependent Lactobacillus bulgaricus D-Lactate dehydrogenase (D-LDHb) catalyses the reversible conversion of pyruvate into D-lactate. Crystals of D-LDHb complexed with NADH were grown and X-ray data collected to 2.2 A. The structure of D-LDHb was solved by molecular replacement using the dimeric Lactobacillus helveticus D-LDH as a model and was refined to an R-factor of 20.7%. The two subunits of the enzyme display strong asymmetry due to different crystal environments. The opening angles of the two catalytic domains with respect to the core coenzyme binding domains differ by 16 degrees. Subunit A is in an "open" conformation typical for a dehydrogenase apo enzyme and subunit B is "closed". The NADH-binding site in subunit A is only 30% occupied, while in subunit B it is fully occupied and there is a sulphate ion in the substrate-binding pocket. A pyruvate molecule has been modelled in the active site and its orientation is in agreement with existing kinetic and structural data. On domain closure, a cluster of hydrophobic residues packs tightly around the methyl group of the modelled pyruvate molecule. At least three residues from this cluster govern the substrate specificity. Substrate binding itself contributes to the stabilisation of domain closure and activation of the enzyme. In pyruvate reduction, D-LDH can adapt another protonated residue, a lysine residue, to accomplish the role of the acid catalyst His296. Required lowering of the lysine pK(a) value is explained on the basis of the H296K mutant structure.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1J49 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_delbrueckii_subsp._bulgaricus Lactobacillus delbrueckii subsp. bulgaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J49 OCA].
</div>
<div class="pdbe-citations 1j49" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus., Razeto A, Kochhar S, Hottinger H, Dauter M, Wilson KS, Lamzin VS, J Mol Biol. 2002 Apr 19;318(1):109-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054772 12054772]
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
[[Category: D-lactate dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactobacillus delbrueckii subsp. bulgaricus]]
[[Category: Lactobacillus delbrueckii subsp. bulgaricus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dauter, M.]]
[[Category: Dauter M]]
[[Category: Hottinger, H.]]
[[Category: Hottinger H]]
[[Category: Kochhar, S.]]
[[Category: Kochhar S]]
[[Category: Lamzin, V S.]]
[[Category: Lamzin VS]]
[[Category: Razeto, A.]]
[[Category: Razeto A]]
[[Category: Wilson, K S.]]
[[Category: Wilson KS]]
[[Category: Last step of glycolysis under anaerobic condition]]
[[Category: Nad-dependent dehydrogenase]]
[[Category: Reversible interconversion of pyruvate into d-lactate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:47:11 2008''
Retrieved from "https://proteopedia.org/1j49"