1soi
From Proteopedia
(New page: 200px<br /><applet load="1soi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1soi, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1soi.gif|left|200px]]<br /><applet load="1soi" size=" | + | [[Image:1soi.gif|left|200px]]<br /><applet load="1soi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1soi, resolution 1.8Å" /> | caption="1soi, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEX WITH SM+3'''<br /> | '''CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEX WITH SM+3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the crystal structure, at 1.4A, of the Nudix hydrolase | + | 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== | ||
| - | 1SOI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with SM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1SOI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=SM:'>SM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: BSGC, Berkeley | + | [[Category: BSGC, Berkeley Structural Genomics Center.]] |
| - | [[Category: Bessman, M | + | [[Category: Bessman, M J.]] |
| - | [[Category: Brenner, S | + | [[Category: Brenner, S E.]] |
| - | [[Category: Hill, E | + | [[Category: Hill, E E.]] |
| - | [[Category: Holbrook, E | + | [[Category: Holbrook, E L.]] |
| - | [[Category: Holbrook, S | + | [[Category: Holbrook, S R.]] |
| - | [[Category: Mooster, J | + | [[Category: Mooster, J L.]] |
[[Category: Ranatunga, W.]] | [[Category: Ranatunga, W.]] | ||
[[Category: Schulze-Gahmen, U.]] | [[Category: Schulze-Gahmen, U.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:39 2008'' |
Revision as of 13:03, 21 February 2008
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CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEX WITH SM+3
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
1SOI is a Single protein structure of sequence from Deinococcus radiodurans with as ligand. 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 15:03:39 2008
Categories: Deinococcus radiodurans | Single protein | BSGC, Berkeley Structural Genomics Center. | Bessman, M J. | Brenner, S E. | Hill, E E. | Holbrook, E L. | Holbrook, S R. | Mooster, J L. | Ranatunga, W. | Schulze-Gahmen, U. | Xu, W. | SM | Alpha-beta-alpha sandwich | Berkeley structural genomics center | Bsgc structure funded by nih | Nudix fold | Protein structure initiative | Psi | Structural genomics
