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1lth

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[[Image:1lth.jpg|left|200px]]
[[Image:1lth.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1lth |SIZE=350|CAPTION= <scene name='initialview01'>1lth</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1lth", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FBP:FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= BIFIDOBACTERIUM LONGUM LDH GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1679 Bifidobacterium longum bv. Longum])
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-->
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|DOMAIN=
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{{STRUCTURE_1lth| PDB=1lth | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lth OCA], [http://www.ebi.ac.uk/pdbsum/1lth PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lth RCSB]</span>
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}}
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'''T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL'''
'''T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL'''
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[[Category: Iwata, S.]]
[[Category: Iwata, S.]]
[[Category: Ohta, T.]]
[[Category: Ohta, T.]]
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[[Category: oxidoreductase (choh(d)-nad(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:16:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:17 2008''
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Revision as of 21:16, 2 May 2008

Image:1lth.jpg

Template:STRUCTURE 1lth

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


Overview

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.

About this Structure

1LTH is a Single protein structure of sequence from Bifidobacterium longum bv. longum. Full crystallographic information is available from 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:7656036 Page seeded by OCA on Sat May 3 00:16:21 2008

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