1EUS

SIALIDASE COMPLEXED WITH 2-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID

Summary for 1EUS

• Entry DOI: 10.2210/pdb1eus/pdb
• Descriptor: SIALIDASE, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID (3 entities in total)
• Functional Keywords: neuraminidase, sialidase, hydrolase
• Biological source: Micromonospora viridifaciens
• Cellular location: Secreted: Q02834
• Total number of polymer chains: 1
• Total formula weight: 39183.96

Authors

Gaskell, A.,Crennell, S.J.,Taylor, G.L. (deposition date: 1996-06-21, release date: 1997-01-11, Last modification date: 2024-02-07)

Primary citation

Gaskell, A.,Crennell, S.,Taylor, G.
The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll.
Structure, 3:1197-1205, 1995

PubMed Abstract: Sialidases, or neuraminidases, have been implicated in the pathogenesis of many diseases, but are also produced by many non-pathogenic bacteria. Bacterial sialidases are very variable in size, often possessing domains in addition to the catalytic domain. The sialidase from the non-pathogenic soil bacterium Micromonospora viridifaciens is secreted in two forms with molecular weights of 41 kDa or 68 kDa, depending on the nature of the carbohydrate used to induce expression.

PubMed: 8591030
DOI: 10.1016/S0969-2126(01)00255-6

Experimental method

X-RAY DIFFRACTION (2 Å)