1lth

From Proteopedia
Revision as of 11:02, 25 November 2020 by OCA (talk | contribs)
Jump to navigation Jump to search

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 bv. 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:, ,
Gene:BIFIDOBACTERIUM LONGUM LDH GENE (Bifidobacterium longum bv. 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Iwata S, Kamata K, Yoshida S, Minowa T, Ohta T. T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control. Nat Struct Biol. 1994 Mar;1(3):176-85. PMID:7656036

1lth, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA