4I42

E.coli. 1,4-dihydroxy-2-naphthoyl coenzyme A synthase (ecMenB) in complex with 1-hydroxy-2-naphthoyl-CoA

Summary for 4I42

• Entry DOI: 10.2210/pdb4i42/pdb
• Related: 4ELX
• Descriptor: 1,4-Dihydroxy-2-naphthoyl-CoA synthase, 1-hydroxy-2-naphthoyl-CoA, 1,2-ETHANEDIOL, ... (10 entities in total)
• Functional Keywords: lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 12
• Total formula weight: 397457.60

Authors

Sun, Y.,Song, H.,Li, J.,Li, Y.,Jiang, M.,Zhou, J.,Guo, Z. (deposition date: 2012-11-27, release date: 2013-05-08, Last modification date: 2023-11-08)

Primary citation

Sun, Y.,Song, H.,Li, J.,Li, Y.,Jiang, M.,Zhou, J.,Guo, Z.
Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme A synthase from the crotonase fold superfamily
Plos One, 8:e63095-e63095, 2013

PubMed Abstract: 1, 4-Dihydroxy-2-naphthoyl coenzyme A (DHNA-CoA) synthase is a typical crotonase fold enzyme with an implicated role of conformational changes in catalysis. We have identified these conformational changes by determining the structures of its Escherichia coli and Synechocystis sp. PCC6803 orthologues in complex with a product analog. The structural changes include the folding of an active-site loop into a β-hairpin and significant reorientation of a helix at the carboxy terminus. Interestingly, a new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand. Site-directed mutation of the amino acid residues involved in these ligand-induced interactions significantly diminishes the enzyme activity. These results suggest a catalytically essential induced-fit that is likely initiated by the enzyme-ligand interactions at the active site.

PubMed: 23658663
DOI: 10.1371/journal.pone.0063095

Experimental method

X-RAY DIFFRACTION (1.848 Å)