1EJD

Crystal structure of unliganded mura (type1)

Summary for 1EJD

• Entry DOI: 10.2210/pdb1ejd/pdb
• Related: 1dgl 1ejc 1naw
• Descriptor: UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYLTRANSFERASE, PHOSPHATE ION, CYCLOHEXYLAMMONIUM ION, ... (4 entities in total)
• Functional Keywords: inside-out alpha/beta barrel, transferase
• Biological source: Enterobacter cloacae
• Cellular location: Cytoplasm (Probable): P33038
• Total number of polymer chains: 2
• Total formula weight: 91584.29

Authors

Eschenburg, S.,Schonbrunn, E. (deposition date: 2000-03-02, release date: 2000-10-25, Last modification date: 2023-08-09)

Primary citation

Eschenburg, S.,Schonbrunn, E.
Comparative X-ray analysis of the un-liganded fosfomycin-target murA.
Proteins, 40:290-298, 2000

PubMed Abstract: MurA, an essential enzyme for the synthesis of the bacterial cell wall, follows an induced-fit mechanism. Upon substrate binding, the active site forms in the interdomain cleft, involving movements of the two domains of the protein and a reorientation of the loop Pro112-Pro121. We compare two structures of un-liganded MurA from Enterobacter cloacae: a new orthorhombic form, solved to 1.80 A resolution, and a monoclinic form, redetermined to 1.55 A resolution. In the monoclinic form, the loop Pro112-Pro121 stretches into solvent, while in the new form it adopts a winded conformation, thereby reducing solvent accessibility of the critical residue Cys115. In the interdomain cleft a network of 27 common water molecules has been identified, which partially shields negative charges in the cleft and stabilizes the orientation of catalytically crucial residues. This could support substrate binding and ease domain movements. Near the hinge region an isoaspartyl residue has been recognized, which is the product of post-translational modification of the genetically encoded Asn67-Gly68. The homogeneous population with L-isoaspartate in both structures suggests that the modification in Enterobacter cloacae MurA is not a mere aging defect but rather the result of a specific in vivo process.

PubMed: 10842342
DOI: 10.1002/(SICI)1097-0134(20000801)40:2<290::AID-PROT90>3.0.CO;2-0

Experimental method

X-RAY DIFFRACTION (1.55 Å)