1ojq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ojq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ojq, resolution 1.68&Aring;" /> '''THE CRYSTAL STRUCTUR...)
Line 1: Line 1:
-
[[Image:1ojq.jpg|left|200px]]<br /><applet load="1ojq" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ojq.jpg|left|200px]]<br /><applet load="1ojq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ojq, resolution 1.68&Aring;" />
caption="1ojq, resolution 1.68&Aring;" />
'''THE CRYSTAL STRUCTURE OF C3STAU2 FROM S. AUREUS'''<br />
'''THE CRYSTAL STRUCTURE OF C3STAU2 FROM S. AUREUS'''<br />
==Overview==
==Overview==
-
The C3stau2 exoenzyme from Staphylococcus aureus is a C3-like, ADP-ribosyltransferase that ADP-ribosylates not only RhoA-C but also, RhoE/Rnd3. In this study we have crystallized and determined the structure, of C3stau2 in both its native form and in complex with NAD at 1.68- and, 2.02-A resolutions, respectively. The topology of C3stau2 is similar to, that of C3bot1 from Clostridium botulinum (with which it shares 35% amino, acid sequence identity) with the addition of two extra helices after, strand beta1. The native structure also features a novel orientation of, the catalytic ARTT loop, which approximates the conformation seen for the, "NAD bound" form of C3bot1. C3stau2 orients NAD similarly to C3bot1, and, on binding NAD, C3stau2 undergoes a clasping motion and a rearrangement of, the phosphate-nicotinamide binding loop, enclosing the NAD in the binding, site. Comparison of these structures with those of C3bot1 and related, toxins reveals a degree of divergence in the interactions with the adenine, moiety among the ADP-ribosylating toxins that contrasts with the more, conserved interactions with the nicotinamide. Comparison with C3bot1 gives, some insight into the different protein substrate specificities of these, enzymes.
+
The C3stau2 exoenzyme from Staphylococcus aureus is a C3-like ADP-ribosyltransferase that ADP-ribosylates not only RhoA-C but also RhoE/Rnd3. In this study we have crystallized and determined the structure of C3stau2 in both its native form and in complex with NAD at 1.68- and 2.02-A resolutions, respectively. The topology of C3stau2 is similar to that of C3bot1 from Clostridium botulinum (with which it shares 35% amino acid sequence identity) with the addition of two extra helices after strand beta1. The native structure also features a novel orientation of the catalytic ARTT loop, which approximates the conformation seen for the "NAD bound" form of C3bot1. C3stau2 orients NAD similarly to C3bot1, and on binding NAD, C3stau2 undergoes a clasping motion and a rearrangement of the phosphate-nicotinamide binding loop, enclosing the NAD in the binding site. Comparison of these structures with those of C3bot1 and related toxins reveals a degree of divergence in the interactions with the adenine moiety among the ADP-ribosylating toxins that contrasts with the more conserved interactions with the nicotinamide. Comparison with C3bot1 gives some insight into the different protein substrate specificities of these enzymes.
==About this Structure==
==About this Structure==
-
1OJQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OJQ OCA].
+
1OJQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJQ OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
-
[[Category: Acharya, K.R.]]
+
[[Category: Acharya, K R.]]
[[Category: Ayriss, J.]]
[[Category: Ayriss, J.]]
-
[[Category: Evans, H.R.]]
+
[[Category: Evans, H R.]]
-
[[Category: Holloway, D.E.]]
+
[[Category: Holloway, D E.]]
-
[[Category: Shone, C.C.]]
+
[[Category: Shone, C C.]]
-
[[Category: Sutton, J.M.]]
+
[[Category: Sutton, J M.]]
[[Category: adp-ribosyltransferase]]
[[Category: adp-ribosyltransferase]]
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:59:18 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:32 2008''

Revision as of 12:18, 21 February 2008


1ojq, resolution 1.68Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE OF C3STAU2 FROM S. AUREUS

Overview

The C3stau2 exoenzyme from Staphylococcus aureus is a C3-like ADP-ribosyltransferase that ADP-ribosylates not only RhoA-C but also RhoE/Rnd3. In this study we have crystallized and determined the structure of C3stau2 in both its native form and in complex with NAD at 1.68- and 2.02-A resolutions, respectively. The topology of C3stau2 is similar to that of C3bot1 from Clostridium botulinum (with which it shares 35% amino acid sequence identity) with the addition of two extra helices after strand beta1. The native structure also features a novel orientation of the catalytic ARTT loop, which approximates the conformation seen for the "NAD bound" form of C3bot1. C3stau2 orients NAD similarly to C3bot1, and on binding NAD, C3stau2 undergoes a clasping motion and a rearrangement of the phosphate-nicotinamide binding loop, enclosing the NAD in the binding site. Comparison of these structures with those of C3bot1 and related toxins reveals a degree of divergence in the interactions with the adenine moiety among the ADP-ribosylating toxins that contrasts with the more conserved interactions with the nicotinamide. Comparison with C3bot1 gives some insight into the different protein substrate specificities of these enzymes.

About this Structure

1OJQ is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

The crystal structure of C3stau2 from Staphylococcus aureus and its complex with NAD., Evans HR, Sutton JM, Holloway DE, Ayriss J, Shone CC, Acharya KR, J Biol Chem. 2003 Nov 14;278(46):45924-30. Epub 2003 Aug 21. PMID:12933793

Page seeded by OCA on Thu Feb 21 14:18:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools