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1lth

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[[Image:1lth.jpg|left|200px]]<br /><applet load="1lth" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lth.jpg|left|200px]]
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caption="1lth, resolution 2.5&Aring;" />
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'''T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL'''<br />
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{{Structure
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|PDB= 1lth |SIZE=350|CAPTION= <scene name='initialview01'>1lth</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FBP:FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=OXM:OXAMIC ACID'>OXM</scene>
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|ACTIVITY= [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]
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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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'''T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LTH 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 <scene name='pdbligand=FBP:'>FBP</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=OXM:'>OXM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTH OCA].
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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==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7656036 7656036]
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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: Bifidobacterium longum bv. longum]]
[[Category: L-lactate dehydrogenase]]
[[Category: L-lactate dehydrogenase]]
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[[Category: oxidoreductase (choh(d)-nad(a))]]
[[Category: oxidoreductase (choh(d)-nad(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:00 2008''

Revision as of 10:35, 20 March 2008

Image:1lth.jpg


PDB ID 1lth

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , and
Gene: BIFIDOBACTERIUM LONGUM LDH GENE (Bifidobacterium longum bv. Longum)
Activity: L-lactate dehydrogenase, with EC number 1.1.1.27
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 12:35:00 2008

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