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5OQ1

Crystal structure of Serratia marcescens ChiX (used as MR model for superior PDB 5OPZ)

Summary for 5OQ1
Entry DOI10.2210/pdb5oq1/pdb
Related5OPZ
DescriptorChiX, ZINC ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsl-ala d-glu endopeptidase serratia marcescens chitinase secretion anomalous dispersion zinc enzyme, hydrolase
Biological sourceSerratia marcescens
Total number of polymer chains2
Total formula weight31135.57
Authors
Owen, R.A.,Fyfe, P.K.,Lodge, A.,Biboy, J.,Vollmer, W.,Hunter, W.N.,Sargent, F. (deposition date: 2017-08-10, release date: 2018-01-17, Last modification date: 2024-05-08)
Primary citationOwen, R.A.,Fyfe, P.K.,Lodge, A.,Biboy, J.,Vollmer, W.,Hunter, W.N.,Sargent, F.
Structure and activity of ChiX: a peptidoglycan hydrolase required for chitinase secretion by Serratia marcescens.
Biochem. J., 475:415-428, 2018
Cited by
PubMed Abstract: The Gram-negative bacterium secretes many proteins that are involved in extracellular chitin degradation. This so-called chitinolytic machinery includes three types of chitinase enzymes and a lytic polysaccharide monooxygenase. An operon has been identified in , , that is thought to be involved in the secretion of the chitinolytic machinery. Genetic evidence points to the ChiX protein being a key player in the secretion mechanism, since deletion of the gene in led to a mutant strain blocked for secretion of all members of the chitinolytic machinery. In this work, a detailed structural and biochemical characterisation of ChiX is presented. The high-resolution crystal structure of ChiX reveals the protein to be a member of the LAS family of peptidases. ChiX is shown to be a zinc-containing metalloenzyme, and assays demonstrate that ChiX is an l-Ala d-Glu endopeptidase that cleaves the cross-links in bacterial peptidoglycan. This catalytic activity is shown to be intimately linked with the secretion of the chitinolytic machinery, since substitution of the ChiX Asp-120 residue results in a variant protein that is both unable to digest peptidoglycan and cannot rescue the phenoytype of a mutant strain.
PubMed: 29229757
DOI: 10.1042/BCJ20170633
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.34 Å)
Structure validation

226707

數據於2024-10-30公開中

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