2sil: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2sil.gif|left|200px]]
{{Seed}}
[[Image:2sil.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2sil|  PDB=2sil  |  SCENE=  }}  
{{STRUCTURE_2sil|  PDB=2sil  |  SCENE=  }}  


'''THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE AND ITS COMPLEX WITH A TRANSITION STATE ANALOGUE AT 1.6 ANGSTROMS RESOLUTION'''
===THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE AND ITS COMPLEX WITH A TRANSITION STATE ANALOGUE AT 1.6 ANGSTROMS RESOLUTION===




==Overview==
<!--
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 occupy the space available. Solvent structure differs only around the third phosphonate oxygen, which attracts a potassium ion. The STNA structure is topologically identical to the previously reported influenza virus neuraminidase structures, although very different in detail; the root-mean-square (r.m.s) deviation for 210 C alpha positions considered equivalent is 2.28 angstroms (out of a total of 390 residues in influenza and 381 in STNA). The active site residues are more highly conserved, in that both the viral and bacterial structures contain an arginine triad, a hydrophobic pocket, a tyrosine and glutamic acid residue at the base of the site and a potential proton-donating aspartic acid. However, differences in binding to O4 and to the glycerol side-chain may reflect the different kinetics employed by the two enzymes.
The line below this paragraph, {{ABSTRACT_PUBMED_8656428}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8656428 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8656428}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Vimr, E R.]]
[[Category: Vimr, E R.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:19:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:54:16 2008''

Revision as of 01:54, 28 July 2008

File:2sil.png

Template:STRUCTURE 2sil

THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE AND ITS COMPLEX WITH A TRANSITION STATE ANALOGUE AT 1.6 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8656428

About this Structure

2SIL is a Single protein structure of sequence from Salmonella typhimurium. This structure supersedes the now removed PDB entry 1sil. Full crystallographic information is available from OCA.

Reference

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 Mon Jul 28 04:54:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2sil&oldid=682023"