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New page: left|200px<br /><applet load="1lth" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lth, resolution 2.5Å" /> '''T AND R STATES IN THE...
 
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[[Image:1lth.jpg|left|200px]]<br /><applet load="1lth" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lth, resolution 2.5&Aring;" />
'''T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL'''<br />


==Overview==
==T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL==
The crystal structure of L-lactate dehydrogenase from Bifidobacterium, longum, determined to 2.5 A resolution, contains a regular 1:1 complex of, T- and R-state tetramers. A comparison of these two structures within the, same crystal lattice and kinetical characterization of the T-R transition, in solution provide an explanation for the molecular mechanism of, allosteric activation. Substrate affinity is controlled by helix sliding, between subunits which is triggered by the binding of the activator, fructose 1,6-bisphosphate. The proposed mechanism can explain activation, by chemical modification and mutagenesis, as well as suggesting why, vertebrate counterparts are not allosteric.
<StructureSection load='1lth' size='340' side='right'caption='[[1lth]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lth]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._longum Bifidobacterium longum subsp. longum]. The June 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Lactate Dehydrogenase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_6 10.2210/rcsb_pdb/mom_2008_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LTH 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</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=1lth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lth OCA], [https://pdbe.org/1lth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lth RCSB], [https://www.ebi.ac.uk/pdbsum/1lth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lth ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LDH2_BIFL2 LDH2_BIFL2] Catalyzes the conversion of lactate to pyruvate.[HAMAP-Rule:MF_00488]
== 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/lt/1lth_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=1lth ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_bv._longum Bifidobacterium longum bv. longum] with FBP, NAD and OXM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LTH OCA].
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control., Iwata S, Kamata K, Yoshida S, Minowa T, Ohta T, Nat Struct Biol. 1994 Mar;1(3):176-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7656036 7656036]
[[Category: Bifidobacterium longum subsp. longum]]
[[Category: Bifidobacterium longum bv. longum]]
[[Category: Lactate Dehydrogenase]]
[[Category: L-lactate dehydrogenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Iwata, S.]]
[[Category: Iwata S]]
[[Category: Ohta, T.]]
[[Category: Ohta T]]
[[Category: FBP]]
[[Category: NAD]]
[[Category: OXM]]
[[Category: oxidoreductase (choh(d)-nad(a))]]
 
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Latest revision as of 07:35, 14 February 2024

T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL

1lth, resolution 2.50Å

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