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4GVG

Crystal structure of Salmonella typhimurium family 3 glycoside hydrolase (NagZ)

Summary for 4GVG
Entry DOI10.2210/pdb4gvg/pdb
Related4GVF 4GVH 4GVI
DescriptorBeta-hexosaminidase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
Functional Keywordstim-barrel, hydrolase
Biological sourceSalmonella enterica subsp. enterica serovar Typhimurium
Cellular locationCytoplasm (By similarity): Q8ZQ06
Total number of polymer chains2
Total formula weight77838.34
Authors
Bacik, J.P.,Mark, B.L. (deposition date: 2012-08-30, release date: 2012-12-19, Last modification date: 2023-09-13)
Primary citationBacik, J.P.,Whitworth, G.E.,Stubbs, K.A.,Vocadlo, D.J.,Mark, B.L.
Active Site Plasticity within the Glycoside Hydrolase NagZ Underlies a Dynamic Mechanism of Substrate Distortion.
Chem.Biol., 19:1471-1482, 2012
Cited by
PubMed Abstract: NagZ is a glycoside hydrolase that participates in peptidoglycan (PG) recycling by removing β-N-acetylglucosamine from PG fragments that are excised from the bacterial cell wall during growth. Notably, the products formed by NagZ, 1,6-anhydroMurNAc-peptides, activate β-lactam resistance in many Gram-negative bacteria, making this enzyme of interest as a potential therapeutic target. Crystal structure determinations of NagZ from Salmonella typhimurium and Bacillus subtilis in complex with natural substrate, trapped as a glycosyl-enzyme intermediate, and bound to product, define the reaction coordinate of the NagZ family of enzymes. The structures, combined with kinetic studies, reveal an uncommon degree of structural plasticity within the active site of a glycoside hydrolase, and unveil how NagZ drives substrate distortion using a highly mobile loop that contains a conserved histidine that has been proposed as the general acid/base.
PubMed: 23177201
DOI: 10.1016/j.chembiol.2012.09.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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數據於2024-11-06公開中

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