| Title | Crystal structure of Spore coat polysaccharide biosynthesis protein spsE (BSU37870) from Bacillus subtilis at 2.38 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 355716 | | Molecular Characteristics | | Source | Bacillus subtilis subsp. subtilis str. 168 | | Alias Ids | TPS1349,2636322 | Molecular Weight | 40887.44 Da. | | Residues | 373 | Isoelectric Point | 5.37 | | Sequence | maafqianktvgkdapvfiiaeaginhdgkldqafalidaaaeagadavkfqmfqadrmyqkdpglykt aagkdvsifslvqsmempaewilplldycrekqviflstvcdegsadllqstspsafkiasyeinhlpl lkyvarlnrpmifstagaeisdvheawrtiraegnnqiaimhcvakypappeysnlsvipmlaaafpea vigfsdhsehpteapcaavrlgakliekhftidknlpgadhsfalnpdelkemvdgirkteaelkqgit kpvsekllgssyktttaiegeirnfayrgifttapiqkgeafsedniavlrpgqkpqglhprffellts gvravrdipadtgivwddillkdspfhe | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 1 | | Resolution (Å) | 2.38 | Rfree | 0.23799 | | Matthews' coefficent | 3.74 | Rfactor | 0.19035 | | Waters | 83 | Solvent Content | 66.82 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The gene 2636322 from Bacillus subtilis encodes a putative N-acetylneuraminic acid (Neu5Ac) synthase EC:2.5.1.57 COG2089, a member of NeuB family PF03102. Alternative names: N-acetylneuraminate 9-phosphate lyase, sialic acid 9-phosphate synthetase. The enzyme belongs to the class of alpha and beta (a+b) proteins and reveals TIM beta/alpha-barrel SCOP51350. The enzyme catalyzes the following reaction: phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H(2)O <=> N-acylneuraminate 9-phosphate + phosphate. Sialic acid or N-acetylneuraminic acid (NeuAc) plays a wide variety of important biological roles. In mammals, it is found as the terminal carbohydrate residue of many cell surface glycoconju- gates. Thus, its structure defines the periphery of mammalian cells, and it is a key determinant in mediating cellular recognition processes. These include the binding between selectins and leukocytes in the inflammation response (5) and the binding of the influenza virus and mammalian cells during infection. While sialic acid is not commonly found in prokaryotes, certain pathogenic bacteria biosynthesize it as a virulence factor [Ref]. Thus, it is an attractive drug target. For instance, the structure of the enzyme homologue from Neisseria meningitidis in complex with its first potent inhibitor has been recently determined 2WQP.
Ligand Summary
References
