4gvh | pdb_00004gvh

Crystal structure of Salmonella typhimurium family 3 glycoside hydrolase (NagZ) covalently bound to 5-fluoro-GlcNAc.

spinqualitylabelsall models 4gvh, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gvh is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium str. lt2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 0XY, MES Related: 4gvf, 4gvg, 4gvi Gene: nagZ, STM1209 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) Activity: Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed NagZ is a glycoside hydrolase that participates in peptidoglycan (PG) recycling by removing beta-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 beta-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. Active Site Plasticity within the Glycoside Hydrolase NagZ Underlies a Dynamic Mechanism of Substrate Distortion.,Bacik JP, Whitworth GE, Stubbs KA, Vocadlo DJ, Mark BL Chem Biol. 2012 Nov 21;19(11):1471-82. doi: 10.1016/j.chembiol.2012.09.016. PMID:23177201 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-Hexosaminidase

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