1hq0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1hq0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hq0, resolution 1.83&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Line 1: Line 1:
-
[[Image:1hq0.jpg|left|200px]]<br /><applet load="1hq0" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1hq0.jpg|left|200px]]<br /><applet load="1hq0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hq0, resolution 1.83&Aring;" />
caption="1hq0, resolution 1.83&Aring;" />
'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF E.COLI CYTOTOXIC NECROTIZING FACTOR TYPE 1'''<br />
'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF E.COLI CYTOTOXIC NECROTIZING FACTOR TYPE 1'''<br />
==Overview==
==Overview==
-
Certain uropathogenic and neonatal meningitis-causing strains of, Escherichia coli express a 114 kDa protein toxin called cytotoxic, necrotizing factor 1 (CNF1). The toxin causes alteration of the host cell, actin cytoskeleton and promotes bacterial invasion of blood-brain barrier, endothelial cells. CNF1 belongs to a unique group of large cytotoxins that, cause constitutive activation of Rho guanosine triphosphatases (GTPases), which are key regulators of the actin cytoskeleton. This group also, includes E. coli cytotoxic necrotizing factor 2 (CNF2, 114 kDa) and, dermonecrotic toxins (DNT, 159 kDa) of Bordetella spp. with related, sequences occurring in Yersinia spp. Here we show that the catalytic, region of CNF1 exhibits a novel protein fold as determined by its 1.83 A, resolution crystal structure. The structure reveals that CNF1 has a, Cys-His-main chain oxygen catalytic triad reminiscent of enzymes belonging, to the catalytic triad superfamily. The position of the catalytic Cys, residue at the base of a deep pocket restricts access to potential, substrates and helps explain the high specificity of this and related, toxins.
+
Certain uropathogenic and neonatal meningitis-causing strains of Escherichia coli express a 114 kDa protein toxin called cytotoxic necrotizing factor 1 (CNF1). The toxin causes alteration of the host cell actin cytoskeleton and promotes bacterial invasion of blood-brain barrier endothelial cells. CNF1 belongs to a unique group of large cytotoxins that cause constitutive activation of Rho guanosine triphosphatases (GTPases), which are key regulators of the actin cytoskeleton. This group also includes E. coli cytotoxic necrotizing factor 2 (CNF2, 114 kDa) and dermonecrotic toxins (DNT, 159 kDa) of Bordetella spp. with related sequences occurring in Yersinia spp. Here we show that the catalytic region of CNF1 exhibits a novel protein fold as determined by its 1.83 A resolution crystal structure. The structure reveals that CNF1 has a Cys-His-main chain oxygen catalytic triad reminiscent of enzymes belonging to the catalytic triad superfamily. The position of the catalytic Cys residue at the base of a deep pocket restricts access to potential substrates and helps explain the high specificity of this and related toxins.
==About this Structure==
==About this Structure==
-
1HQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQ0 OCA].
+
1HQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQ0 OCA].
==Reference==
==Reference==
Line 23: Line 23:
[[Category: rho transglutaminase]]
[[Category: rho transglutaminase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:54:20 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:45 2008''

Revision as of 11:03, 21 February 2008


1hq0, resolution 1.83Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF E.COLI CYTOTOXIC NECROTIZING FACTOR TYPE 1

Overview

Certain uropathogenic and neonatal meningitis-causing strains of Escherichia coli express a 114 kDa protein toxin called cytotoxic necrotizing factor 1 (CNF1). The toxin causes alteration of the host cell actin cytoskeleton and promotes bacterial invasion of blood-brain barrier endothelial cells. CNF1 belongs to a unique group of large cytotoxins that cause constitutive activation of Rho guanosine triphosphatases (GTPases), which are key regulators of the actin cytoskeleton. This group also includes E. coli cytotoxic necrotizing factor 2 (CNF2, 114 kDa) and dermonecrotic toxins (DNT, 159 kDa) of Bordetella spp. with related sequences occurring in Yersinia spp. Here we show that the catalytic region of CNF1 exhibits a novel protein fold as determined by its 1.83 A resolution crystal structure. The structure reveals that CNF1 has a Cys-His-main chain oxygen catalytic triad reminiscent of enzymes belonging to the catalytic triad superfamily. The position of the catalytic Cys residue at the base of a deep pocket restricts access to potential substrates and helps explain the high specificity of this and related toxins.

About this Structure

1HQ0 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1., Buetow L, Flatau G, Chiu K, Boquet P, Ghosh P, Nat Struct Biol. 2001 Jul;8(7):584-8. PMID:11427886

Page seeded by OCA on Thu Feb 21 13:03:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools