1lsp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1lsp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lsp, resolution 2.45&Aring;" /> '''THE CRYSTAL STRUCTUR...)
Line 1: Line 1:
-
[[Image:1lsp.jpg|left|200px]]<br /><applet load="1lsp" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1lsp.jpg|left|200px]]<br /><applet load="1lsp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lsp, resolution 2.45&Aring;" />
caption="1lsp, resolution 2.45&Aring;" />
'''THE CRYSTAL STRUCTURE OF A BULGECIN-INHIBITED G-TYPE LYSOZYME FROM THE EGG-WHITE OF THE AUSTRALIAN BLACK SWAN. A COMPARISON OF THE BINDING OF BULGECIN TO THREE MURAMIDASES'''<br />
'''THE CRYSTAL STRUCTURE OF A BULGECIN-INHIBITED G-TYPE LYSOZYME FROM THE EGG-WHITE OF THE AUSTRALIAN BLACK SWAN. A COMPARISON OF THE BINDING OF BULGECIN TO THREE MURAMIDASES'''<br />
==Overview==
==Overview==
-
Bulgecin A, a bacterial metabolite, has been shown to bind in the, active-site groove of the chicken-type lysozyme from the rainbow trout, (RBTL) and in the lysozyme-like C-terminal domain, of a soluble lytic, transglycosylase (C-SLT) from Escherichia coli. These enzymes are, muramidases that cleave the glycosidic bonds in the glycan strands of the, murein polymer. Here we report the crystal structure of a complex between, the goose-type lysozyme from the egg white of the Australian black swan, (SEWL) and bulgecin A at 2.45 A resolution. As is the case for the, C-SLT/bulgecin and RBTL/bulgecin complexes, the ligand binds with the, N-acetylglucosamine ring in subsite C and the proline moiety in site D, where it interacts with the catalytic glutamic acid. The taurine residue, interacts with the beta-sheet region. Comparisons of the three buigecin, complexes show that the inhibitor has the same binding mode to the, muramidases with similar protein-ligand interactions, particularly for, SEWL and RBTL. From our results, it seems likely that bulgecin, in, general, inhibits enzymes with lysozyme-like domains and thus might, represent a novel class of natural antibiotics that act on, murein-degrading rather than murein-synthesizing enzymes.
+
Bulgecin A, a bacterial metabolite, has been shown to bind in the active-site groove of the chicken-type lysozyme from the rainbow trout (RBTL) and in the lysozyme-like C-terminal domain, of a soluble lytic transglycosylase (C-SLT) from Escherichia coli. These enzymes are muramidases that cleave the glycosidic bonds in the glycan strands of the murein polymer. Here we report the crystal structure of a complex between the goose-type lysozyme from the egg white of the Australian black swan (SEWL) and bulgecin A at 2.45 A resolution. As is the case for the C-SLT/bulgecin and RBTL/bulgecin complexes, the ligand binds with the N-acetylglucosamine ring in subsite C and the proline moiety in site D where it interacts with the catalytic glutamic acid. The taurine residue interacts with the beta-sheet region. Comparisons of the three buigecin complexes show that the inhibitor has the same binding mode to the muramidases with similar protein-ligand interactions, particularly for SEWL and RBTL. From our results, it seems likely that bulgecin, in general, inhibits enzymes with lysozyme-like domains and thus might represent a novel class of natural antibiotics that act on murein-degrading rather than murein-synthesizing enzymes.
==About this Structure==
==About this Structure==
-
1LSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cygnus_atratus Cygnus atratus] with BUL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LSP OCA].
+
1LSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cygnus_atratus Cygnus atratus] with <scene name='pdbligand=BUL:'>BUL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSP OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Hough, E.]]
[[Category: Hough, E.]]
-
[[Category: Isaacs, N.W.]]
+
[[Category: Isaacs, N W.]]
[[Category: Karlsen, S.]]
[[Category: Karlsen, S.]]
-
[[Category: Rao, Z.H.]]
+
[[Category: Rao, Z H.]]
[[Category: BUL]]
[[Category: BUL]]
[[Category: hydrolase (o-glycosyl)]]
[[Category: hydrolase (o-glycosyl)]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:50:48 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:05 2008''

Revision as of 11:48, 21 February 2008


1lsp, resolution 2.45Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE OF A BULGECIN-INHIBITED G-TYPE LYSOZYME FROM THE EGG-WHITE OF THE AUSTRALIAN BLACK SWAN. A COMPARISON OF THE BINDING OF BULGECIN TO THREE MURAMIDASES

Overview

Bulgecin A, a bacterial metabolite, has been shown to bind in the active-site groove of the chicken-type lysozyme from the rainbow trout (RBTL) and in the lysozyme-like C-terminal domain, of a soluble lytic transglycosylase (C-SLT) from Escherichia coli. These enzymes are muramidases that cleave the glycosidic bonds in the glycan strands of the murein polymer. Here we report the crystal structure of a complex between the goose-type lysozyme from the egg white of the Australian black swan (SEWL) and bulgecin A at 2.45 A resolution. As is the case for the C-SLT/bulgecin and RBTL/bulgecin complexes, the ligand binds with the N-acetylglucosamine ring in subsite C and the proline moiety in site D where it interacts with the catalytic glutamic acid. The taurine residue interacts with the beta-sheet region. Comparisons of the three buigecin complexes show that the inhibitor has the same binding mode to the muramidases with similar protein-ligand interactions, particularly for SEWL and RBTL. From our results, it seems likely that bulgecin, in general, inhibits enzymes with lysozyme-like domains and thus might represent a novel class of natural antibiotics that act on murein-degrading rather than murein-synthesizing enzymes.

About this Structure

1LSP is a Single protein structure of sequence from Cygnus atratus with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases., Karlsen S, Hough E, Rao ZH, Isaacs NW, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):105-14. PMID:15299731

Page seeded by OCA on Thu Feb 21 13:48:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools