1dim: Difference between revisions
No edit summary |
No edit summary |
||
| Line 25: | Line 25: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:01:24 2007'' | ||
Revision as of 15:56, 30 October 2007
|
SIALIDASE FROM SALMONELLA TYPHIMURIUM COMPLEXED WITH EPANA INHIBITOR
OverviewOverview
The structure of Salmonella typhimurium LT2 neuraminidase (STNA) is, reported here to a resolution of 1.6 angstroms together with the, structures of three complexes of STNA with different inhibitors. The first, is 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid (Neu5Ac2en or DANA), the, second and third are phosphonate derivatives of N-acetyl-neuraminic acid, (NANA) which have phosphonate groups at the C2 position equatorial (ePANA), and axial (aPANA) to the plane of the sugar ring. The complex structures, are at resolutions of 1.6 angstroms, 1.6 angstroms and 1.9 angstroms, respectively. These analyses show the STNA active site to be topologically, inflexible and the interactions to be dominated by the arginine triad, with the pyranose rings of the inhibitors undergoing distortion to ... [(full description)]
About this StructureAbout this Structure
1DIM is a [Single protein] structure of sequence from [Salmonella typhimurium] with K and EQP as [ligands]. Active as [Exo-alpha-sialidase], with EC number [3.2.1.18]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution., Crennell SJ, Garman EF, Philippon C, Vasella A, Laver WG, Vimr ER, Taylor GL, J Mol Biol. 1996 Jun 7;259(2):264-80. PMID:8656428
Page seeded by OCA on Tue Oct 30 15:01:24 2007