1sly: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1sly.jpg|left|200px]]
{{Seed}}
[[Image:1sly.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sly|  PDB=1sly  |  SCENE=  }}  
{{STRUCTURE_1sly|  PDB=1sly  |  SCENE=  }}  


'''COMPLEX OF THE 70-KDA SOLUBLE LYTIC TRANSGLYCOSYLASE WITH BULGECIN A'''
===COMPLEX OF THE 70-KDA SOLUBLE LYTIC TRANSGLYCOSYLASE WITH BULGECIN A===




==Overview==
<!--  
Bulgecins are O-sulfonated glycopeptides that are able to enhance the antibacterial activity of beta-lactam antibiotics. The 70-kDa soluble lytic transglycosylase (SLT70) from Escherichia coli forms a specific target of these compounds. Using X-ray crystallography, the three-dimensional structure of a complex of SLT70 with bulgecin A has been determined to 2.8-A resolution and refined to an R factor of 19.5%. The model contains all 618 amino acids of SLT70 and a single molecule of bound bulgecin, located in the active site of the enzyme. The glycopeptide inhibitor is bound in an extended conformation occupying sites analogous to the B, C, and D subsites of lysozyme. Upon binding of bulgecin, the three-stranded antiparallel beta-sheet in the C domain shows a pronounced shift toward the inhibitor. In subsite D, the proposed catalytic residue Glu478 forms a hydrogen bond to the hydroxymethyl oxygen of the proline part of bulgecin and interacts electrostatically with the proline NH2+ group. These interactions, in addition to the interactions observed for the 2-acetamido group of the N-acetylglucosamine residue bound in subsite C, may explain the strong inhibition of SLT70 activity by bulgecin, suggesting that bulgecin acts as an analogue of an oxocarbonium ion intermediate in the reaction catalyzed by SLT70. The structure of the SLT70--bulgecin A complex may be of assistance in the rational design of novel antibiotics.
The line below this paragraph, {{ABSTRACT_PUBMED_7548026}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7548026 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7548026}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Peptidoglycan]]
[[Category: Peptidoglycan]]
[[Category: Periplasmic]]
[[Category: Periplasmic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:52:12 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:23:01 2008''

Revision as of 13:23, 28 July 2008

File:1sly.png

Template:STRUCTURE 1sly

COMPLEX OF THE 70-KDA SOLUBLE LYTIC TRANSGLYCOSYLASE WITH BULGECIN A

Template:ABSTRACT PUBMED 7548026

About this Structure

1SLY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism., Thunnissen AM, Rozeboom HJ, Kalk KH, Dijkstra BW, Biochemistry. 1995 Oct 3;34(39):12729-37. PMID:7548026

Page seeded by OCA on Mon Jul 28 16:23:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1sly&oldid=706834"