5JZ9

Crystal structure of HsaD bound to 3,5-dichloro-4-hydroxybenzenesulphonic acid

Summary for 5JZ9

• Entry DOI: 10.2210/pdb5jz9/pdb
• Related: 2VF2
• Descriptor: 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase, 3,5-dichloro-4-hydroxybenzene-1-sulfonic acid (3 entities in total)
• Functional Keywords: hsad, m. tuberculosis, cholesterol, inhibitor, mcp-hydrolase, hydrolase
• Biological source: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
• Total number of polymer chains: 2
• Total formula weight: 62677.11

Authors

Ryan, A.,Polycarpou, E.,Lack, N.A.,Evangelopoulos, D.,Sieg, C.,Halman, A.,Bhakta, S.,Sinclair, A.,Eleftheriadou, O.,McHugh, T.D.,Keany, S.,Lowe, E.,Ballet, R.,Abihammad, A.,Ciulli, A.,Sim, E. (deposition date: 2016-05-16, release date: 2017-04-05, Last modification date: 2024-01-10)

Primary citation

Ryan, A.,Polycarpou, E.,Lack, N.A.,Evangelopoulos, D.,Sieg, C.,Halman, A.,Bhakta, S.,Eleftheriadou, O.,McHugh, T.D.,Keany, S.,Lowe, E.D.,Ballet, R.,Abuhammad, A.,Jacobs, W.R.,Ciulli, A.,Sim, E.
Investigation of the mycobacterial enzyme HsaD as a potential novel target for anti-tubercular agents using a fragment-based drug design approach.
Br. J. Pharmacol., 174:2209-2224, 2017

PubMed Abstract: With the emergence of extensively drug-resistant tuberculosis, there is a need for new anti-tubercular drugs that work through novel mechanisms of action. The meta cleavage product hydrolase, HsaD, has been demonstrated to be critical for the survival of Mycobacterium tuberculosis in macrophages and is encoded in an operon involved in cholesterol catabolism, which is identical in M. tuberculosis and M. bovis BCG.

PubMed: 28380256
DOI: 10.1111/bph.13810

Experimental method

X-RAY DIFFRACTION (2.68 Å)