1lld: Difference between revisions

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New page: left|200px<br /><applet load="1lld" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lld, resolution 2.0Å" /> '''MOLECULAR BASIS OF AL...
 
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[[Image:1lld.gif|left|200px]]<br /><applet load="1lld" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lld, resolution 2.0&Aring;" />
'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE'''<br />


==Overview==
==MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE==
The three-dimensional structure of allosteric L-lactate dehydrogenase from, Bifidobacterium longum, the first example of a T-state structure of, L-lactate dehydrogenase, has been determined to 2.0 A. A comparative study, of this structure with the previously reported R-state structure from, Bacillus stearothermophilus has revealed the allosteric activation, mechanism of the bacterial L-lactate dehydrogenase. The fructose, 1,6-bisphosphate-induced conformational change at the effector site and, the substrate affinity change at the activity site are clearly shown at a, molecular level. Coupling of these changes can be simply explained by a, set of concerted rotations between subunits in the tetramer of the enzyme., This T to R transition is the first example for a tetrameric allosteric, protein where the rotations occur around each of three axes of symmetry.
<StructureSection load='1lld' size='340' side='right'caption='[[1lld]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lld]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._longum Bifidobacterium longum subsp. longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLD 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&#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></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=1lld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lld OCA], [https://pdbe.org/1lld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lld RCSB], [https://www.ebi.ac.uk/pdbsum/1lld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lld 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/ll/1lld_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=1lld ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LLD 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 NAD as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1LLD OCA].
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase., Iwata S, Ohta T, J Mol Biol. 1993 Mar 5;230(1):21-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8450537 8450537]
[[Category: Bifidobacterium longum subsp. longum]]
[[Category: Bifidobacterium longum bv. longum]]
[[Category: Large Structures]]
[[Category: L-lactate dehydrogenase]]
[[Category: Iwata S]]
[[Category: Single protein]]
[[Category: Ohta T]]
[[Category: Iwata, S.]]
[[Category: Ohta, T.]]
[[Category: NAD]]
[[Category: oxidoreductase(choh (d)-nad (a))]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:39:11 2007''

Latest revision as of 10:34, 14 February 2024

MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASEMOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE

Structural highlights

1lld is a 2 chain structure with sequence from Bifidobacterium longum subsp. longum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LDH2_BIFL2 Catalyzes the conversion of lactate to pyruvate.[HAMAP-Rule:MF_00488]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1lld, resolution 2.00Å

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