1lth: Difference between revisions

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[[Image:1lth.png|left|200px]]


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==T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL==
The line below this paragraph, containing "STRUCTURE_1lth", creates the "Structure Box" on the page.
<StructureSection load='1lth' size='340' side='right'caption='[[1lth]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_1lth|  PDB=1lth |  SCENE= }}
<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>


===T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL===
==See Also==
 
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
 
__TOC__
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</StructureSection>
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[[Category: Bifidobacterium longum subsp. longum]]
(as it appears on PubMed at http://www.pubmed.gov), where 7656036 is the PubMed ID number.
[[Category: Lactate Dehydrogenase]]
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[[Category: Large Structures]]
{{ABSTRACT_PUBMED_7656036}}
[[Category: RCSB PDB Molecule of the Month]]
 
[[Category: Iwata S]]
==About this Structure==
[[Category: Ohta T]]
1LTH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_bv._longum Bifidobacterium longum bv. longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTH OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/7656036 7656036]
[[Category: Bifidobacterium longum bv. longum]]
[[Category: L-lactate dehydrogenase]]
[[Category: Single protein]]
[[Category: Iwata, S.]]
[[Category: Ohta, T.]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:10:36 2008''

Latest revision as of 10:35, 14 February 2024

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

Structural highlights

1lth is a 2 chain structure with sequence from Bifidobacterium longum subsp. longum. The June 2008 RCSB PDB Molecule of the Month feature on Lactate Dehydrogenase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2008_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
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

1lth, resolution 2.50Å

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