1lth | pdb_00001lth

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

spinqualitylabelsall models 1lth, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lth is a 2 chain structure with sequence from Bifidobacterium longum biovar 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. Ligands: FBP, NAD, OXM Gene: BIFIDOBACTERIUM LONGUM LDH GENE (Bifidobacterium longum biovar Longum) Activity: L-lactate dehydrogenase, with EC number 1.1.1.27 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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