We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1lth

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:35, 14 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lth.jpg|left|200px]]
 
-
<!--
+
==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>
-
-->
+
<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__
-
==Overview==
+
</StructureSection>
-
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.
+
[[Category: Bifidobacterium longum subsp. longum]]
-
 
+
[[Category: Lactate Dehydrogenase]]
-
==About this Structure==
+
[[Category: Large Structures]]
-
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].
+
[[Category: RCSB PDB Molecule of the Month]]
-
 
+
[[Category: Iwata S]]
-
==Reference==
+
[[Category: Ohta T]]
-
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 Sat May 3 00:16:21 2008''
+

Current revision

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

PDB ID 1lth

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lth"
Personal tools