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1lld
From Proteopedia
(Difference between revisions)
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<StructureSection load='1lld' size='340' side='right'caption='[[1lld]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1lld' size='340' side='right'caption='[[1lld]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1lld]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id=' | + | <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> | <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> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LDH2_BIFL2 LDH2_BIFL2] Catalyzes the conversion of lactate to pyruvate.[HAMAP-Rule:MF_00488] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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:8450537<ref>PMID:8450537</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1lld" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]] | *[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bifidobacterium longum | + | [[Category: Bifidobacterium longum subsp. longum]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Iwata | + | [[Category: Iwata S]] |
| - | [[Category: Ohta | + | [[Category: Ohta T]] |
| - | + | ||
Current revision
MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE
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