1sjy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1sjy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sjy, resolution 1.39&Aring;" /> '''Crystal Structure of...)
Line 1: Line 1:
-
[[Image:1sjy.gif|left|200px]]<br /><applet load="1sjy" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1sjy.gif|left|200px]]<br /><applet load="1sjy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sjy, resolution 1.39&Aring;" />
caption="1sjy, resolution 1.39&Aring;" />
'''Crystal Structure of NUDIX HYDROLASE DR1025 FROM DEINOCOCCUS RADIODURANS'''<br />
'''Crystal Structure of NUDIX HYDROLASE DR1025 FROM DEINOCOCCUS RADIODURANS'''<br />
==Overview==
==Overview==
-
We have determined the crystal structure, at 1.4A, of the Nudix hydrolase, DR1025 from the extremely radiation resistant bacterium Deinococcus, radiodurans. The protein forms an intertwined homodimer by exchanging, N-terminal segments between chains. We have identified additional, conserved elements of the Nudix fold, including the metal-binding motif, a, kinked beta-strand characterized by a proline two positions upstream of, the Nudix consensus sequence, and participation of the N-terminal, extension in the formation of the substrate-binding pocket. Crystal, structures were also solved of DR1025 crystallized in the presence of, magnesium and either a GTP analog or Ap(4)A (both at 1.6A resolution). In, the Ap(4)A co-crystal, the electron density indicated that the product of, asymmetric hydrolysis, ATP, was bound to the enzyme. The GTP analog bound, structure showed that GTP was bound almost identically as ATP. Neither, nucleoside triphosphate was further cleaved.
+
We have determined the crystal structure, at 1.4A, of the Nudix hydrolase DR1025 from the extremely radiation resistant bacterium Deinococcus radiodurans. The protein forms an intertwined homodimer by exchanging N-terminal segments between chains. We have identified additional conserved elements of the Nudix fold, including the metal-binding motif, a kinked beta-strand characterized by a proline two positions upstream of the Nudix consensus sequence, and participation of the N-terminal extension in the formation of the substrate-binding pocket. Crystal structures were also solved of DR1025 crystallized in the presence of magnesium and either a GTP analog or Ap(4)A (both at 1.6A resolution). In the Ap(4)A co-crystal, the electron density indicated that the product of asymmetric hydrolysis, ATP, was bound to the enzyme. The GTP analog bound structure showed that GTP was bound almost identically as ATP. Neither nucleoside triphosphate was further cleaved.
==About this Structure==
==About this Structure==
-
1SJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SJY OCA].
+
1SJY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJY OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
+
[[Category: BSGC, Berkeley Structural Genomics Center.]]
-
[[Category: Bessman, M.J.]]
+
[[Category: Bessman, M J.]]
-
[[Category: Brenner, S.E.]]
+
[[Category: Brenner, S E.]]
-
[[Category: Hill, E.E.]]
+
[[Category: Hill, E E.]]
-
[[Category: Holbrook, E.L.]]
+
[[Category: Holbrook, E L.]]
-
[[Category: Holbrook, S.R.]]
+
[[Category: Holbrook, S R.]]
-
[[Category: Mooster, J.L.]]
+
[[Category: Mooster, J L.]]
[[Category: Ranatunga, W.]]
[[Category: Ranatunga, W.]]
[[Category: Schulze-Gahmen, U.]]
[[Category: Schulze-Gahmen, U.]]
Line 31: Line 31:
[[Category: structural genomics]]
[[Category: structural genomics]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:39:58 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:16 2008''

Revision as of 13:02, 21 February 2008


1sjy, resolution 1.39Å

Drag the structure with the mouse to rotate

Crystal Structure of NUDIX HYDROLASE DR1025 FROM DEINOCOCCUS RADIODURANS

Overview

We have determined the crystal structure, at 1.4A, of the Nudix hydrolase DR1025 from the extremely radiation resistant bacterium Deinococcus radiodurans. The protein forms an intertwined homodimer by exchanging N-terminal segments between chains. We have identified additional conserved elements of the Nudix fold, including the metal-binding motif, a kinked beta-strand characterized by a proline two positions upstream of the Nudix consensus sequence, and participation of the N-terminal extension in the formation of the substrate-binding pocket. Crystal structures were also solved of DR1025 crystallized in the presence of magnesium and either a GTP analog or Ap(4)A (both at 1.6A resolution). In the Ap(4)A co-crystal, the electron density indicated that the product of asymmetric hydrolysis, ATP, was bound to the enzyme. The GTP analog bound structure showed that GTP was bound almost identically as ATP. Neither nucleoside triphosphate was further cleaved.

About this Structure

1SJY is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.

Reference

Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes., Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR, J Mol Biol. 2004 May 21;339(1):103-16. PMID:15123424

Page seeded by OCA on Thu Feb 21 15:02:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools