6ckm

N. meningitidis CMP-sialic acid synthetase in the presence of CMP-sialic acid and Ca2+

spinqualitylabelsall models 6ckm, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ckm is a 1 chain structure with sequence from Neisseria meningitidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.543Å Ligands: CA, GOL, NCC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NEUA_NEIME Publication Abstract from PubMed Cytidine 5'-monophosphate (CMP)-sialic acid synthetase (CSS) is an essential enzyme involved in the biosynthesis of carbohydrates and glycoconjugates containing sialic acids, a class of alpha-keto acids that are generally terminal key recognition residues by many proteins that play important biological and pathological roles. The CSS from Neisseria meningitidis (NmCSS) has been commonly used with other enzymes such as sialic acid aldolase and/or sialyltransferase in synthesizing a diverse array of compounds containing sialic acid or its naturally occurring and non-natural derivatives. To better understand its catalytic mechanism and substrate promiscuity, four NmCSS crystal structures trapped at various stages of the catalytic cycle with bound substrates, substrate analogues, and products have been obtained and are presented here. These structures suggest a mechanism for an "open" and "closed" conformational transition that occurs as sialic acid binds to the NmCSS/cytidine-5'-triphosphate (CTP) complex. The closed conformation positions critical residues to help facilitate the nucleophilic attack of sialic acid C2-OH to the alpha-phosphate of CTP, which is also aided by two observed divalent cations. Product formation drives the active site opening, promoting the release of products. Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography.,Matthews MM, McArthur JB, Li Y, Yu H, Chen X, Fisher AJ Biochemistry. 2019 Oct 4. doi: 10.1021/acs.biochem.9b00517. PMID:31583886 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA