1H05

3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SULPHATE

Summary for 1H05

• Entry DOI: 10.2210/pdb1h05/pdb
• Related: 2DHQ
• Descriptor: 3-DEHYDROQUINATE DEHYDRATASE, SULFATE ION (3 entities in total)
• Functional Keywords: dehydratase, shikimate pathway, alpha/beta protein, lyase, aromatic amino acid biosynthesis
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 1
• Total formula weight: 16060.99

Authors

Roszak, A.W.,Coggins, J.R.,Lapthorn, A.J. (deposition date: 2002-06-11, release date: 2002-10-24, Last modification date: 2023-12-13)

Primary citation

Evans, L.,Roszak, A.W.,Noble, L.,Robinson, D.,Chalk, P.,Matthews, J.,Coggins, J.R.,Price, N.,Lapthorn, A.J.
Specificity of Substrate Recognition by Type II Dehydroquinases as Revealed by Binding of Polyanions(1)
FEBS Lett., 530:24-, 2002

PubMed Abstract: The interactions between the polyanionic ligands phosphate and sulphate and the type II dehydroquinases from Streptomyces coelicolor and Mycobacterium tuberculosis have been characterised using a combination of structural and kinetic methods. From both approaches, it is clear that interactions are more complex in the case of the latter enzyme. The data provide new insights into the differences between the two enzymes in terms of substrate recognition and catalytic efficiency and may also explain the relative potencies of rationally designed inhibitors. An improved route to the synthesis of the substrate 3-dehydroquinic acid (dehydroquinate) is described.

PubMed: 12387860
DOI: 10.1016/S0014-5793(02)03346-X

Experimental method

X-RAY DIFFRACTION (1.5 Å)