4APA

Crystal structure of Mycobacterium tuberculosis fumarase (Rv1098c) S318A in apo form

Summary for 4APA

• Entry DOI: 10.2210/pdb4apa/pdb
• Related: 4ADL 4ADM 4APB
• Descriptor: FUMARATE HYDRATASE CLASS II (2 entities in total)
• Functional Keywords: hydrolase, metabolism
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Cellular location: Cytoplasm (By similarity): O53446
• Total number of polymer chains: 4
• Total formula weight: 200406.64

Authors

Bellinzoni, M.,Haouz, A.,Mechaly, A.E.,Alzari, P.M. (deposition date: 2012-03-31, release date: 2012-04-25, Last modification date: 2023-12-20)

Primary citation

Mechaly, A.E.,Haouz, A.,Miras, I.,Barilone, N.,Weber, P.,Shepard, W.,Alzari, P.M.,Bellinzoni, M.
Conformational Changes Upon Ligand Binding in the Essential Class II Fumarase Rv1098C from Mycobacterium Tuberculosis.
FEBS Lett., 586:1606-, 2012

PubMed Abstract: rv1098c, an essential gene in Mycobacterium tuberculosis, codes for a class II fumarase. We describe here the crystal structure of Rv1098c in complex with l-malate, fumarate or the competitive inhibitor meso-tartrate. The models reveal that substrate binding promotes the closure of the active site through conformational changes involving the catalytic SS-loop and the C-terminal domain, which likely represents a general feature of this enzyme superfamily. Analysis of ligand-enzyme interactions as well as site-directed mutagenesis suggest Ser318 as one of the two acid-base catalysts.

PubMed: 22561013
DOI: 10.1016/J.FEBSLET.2012.04.034

Experimental method

X-RAY DIFFRACTION (2.04 Å)