1j3b: Difference between revisions

Revision as of 14:26, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1j3b.png

Template:STRUCTURE 1j3b

Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8

Template:ABSTRACT PUBMED 16239727

About this StructureAbout this Structure

1J3B is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8 showing the structural basis of induced fit and thermostability., Sugahara M, Ohshima N, Ukita Y, Sugahara M, Kunishima N, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1500-7. Epub 2005, Oct 19. PMID:16239727

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

OCA

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-'''Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8'''
+===Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8===
-==Overview==
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-In order to understand the induced fit and the thermostabilization mechanisms of ATP-dependent phosphoenolpyruvate carboxykinase, the crystal structure of the enzyme from the extreme thermophile Thermus thermophilus HB8 (TtPEPCK) was determined and compared with those of orthologues of known structure from two mesophilic organisms. The protomer structures in these orthologues, which exhibit open/closed interdomain conformations, are similar. Isomorphous crystals of unliganded and ATP-bound TtPEPCK were obtained. The asymmetric units of both crystal forms contain two protomers A and B with closed and open conformations, respectively. ATP was only observed in the interdomain cleft of the closed protomer, suggesting that the induced fit of TtPEPCK agrees with the so-called ;conformational selection' mechanism where ligand binding is not essential for domain closure although its binding leads to the stabilization of the closed state. A bound calcium observed in the N-terminal domain of TtPEPCK probably contributes to the thermal stability. A combination of hydrophobic effects, ion pairs and entropic effects might also contribute to the thermostability of TtPEPCK.
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 ==About this Structure==
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 [[Category: Structural genomic]]
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