1u0j
From Proteopedia
(New page: 200px<br /><applet load="1u0j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u0j, resolution 2.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:1u0j.jpg|left|200px]]<br /><applet load="1u0j" size=" | + | [[Image:1u0j.jpg|left|200px]]<br /><applet load="1u0j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u0j, resolution 2.10Å" /> | caption="1u0j, resolution 2.10Å" /> | ||
'''Crystal Structure of AAV2 Rep40-ADP complex'''<br /> | '''Crystal Structure of AAV2 Rep40-ADP complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the structure of adeno-associated virus type 2 (AAV2) | + | We have determined the structure of adeno-associated virus type 2 (AAV2) Rep40 to 2.1-A resolution with ADP bound at the active site. The complex crystallizes as a monomer with one ADP molecule positioned in an unexpectedly open binding site. The nucleotide-binding pocket consists of the P-loop residues interacting with the phosphates and a loop (nucleoside-binding loop) that emanates from the last strand of the central beta-sheet and interacts with the sugar and base. As a result of the open nature of the binding site, one face of the adenine ring is completely exposed to the solvent, and consequently the number of protein-nucleotide contacts is scarce as compared with other P-loop nucleotide phosphohydrolases. The conformation of the ADP molecule in its binding site bears a resemblance to those found in only three other families of P-loop ATPases: the ATP-binding cassette transporter family, the bacterial RecA proteins, and the type II topoisomerase family. In all these cases, oligomerization is required to attain a competent nucleotide-binding pocket. We propose that this characteristic is native to superfamily 3 helicases and allows for an additional mechanism of regulation by these multifunctional proteins. Furthermore, it explains the strong tendency by members of this family such as simian virus 40 TAg to oligomerize after binding ATP. |
==About this Structure== | ==About this Structure== | ||
| - | 1U0J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Adeno-associated_virus_2 Adeno-associated virus 2] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1U0J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Adeno-associated_virus_2 Adeno-associated virus 2] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U0J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Adeno-associated virus 2]] | [[Category: Adeno-associated virus 2]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Aggarwal, A | + | [[Category: Aggarwal, A K.]] |
| - | [[Category: Escalante, C | + | [[Category: Escalante, C R.]] |
| - | [[Category: James, J | + | [[Category: James, J A.]] |
| - | [[Category: Linden, R | + | [[Category: Linden, R M.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: aaa+ protein]] | [[Category: aaa+ protein]] | ||
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[[Category: p-loop atpases]] | [[Category: p-loop atpases]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:20 2008'' |
Revision as of 13:19, 21 February 2008
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Crystal Structure of AAV2 Rep40-ADP complex
Overview
We have determined the structure of adeno-associated virus type 2 (AAV2) Rep40 to 2.1-A resolution with ADP bound at the active site. The complex crystallizes as a monomer with one ADP molecule positioned in an unexpectedly open binding site. The nucleotide-binding pocket consists of the P-loop residues interacting with the phosphates and a loop (nucleoside-binding loop) that emanates from the last strand of the central beta-sheet and interacts with the sugar and base. As a result of the open nature of the binding site, one face of the adenine ring is completely exposed to the solvent, and consequently the number of protein-nucleotide contacts is scarce as compared with other P-loop nucleotide phosphohydrolases. The conformation of the ADP molecule in its binding site bears a resemblance to those found in only three other families of P-loop ATPases: the ATP-binding cassette transporter family, the bacterial RecA proteins, and the type II topoisomerase family. In all these cases, oligomerization is required to attain a competent nucleotide-binding pocket. We propose that this characteristic is native to superfamily 3 helicases and allows for an additional mechanism of regulation by these multifunctional proteins. Furthermore, it explains the strong tendency by members of this family such as simian virus 40 TAg to oligomerize after binding ATP.
About this Structure
1U0J is a Single protein structure of sequence from Adeno-associated virus 2 with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of adeno-associated virus type 2 Rep40-ADP complex: insight into nucleotide recognition and catalysis by superfamily 3 helicases., James JA, Aggarwal AK, Linden RM, Escalante CR, Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12455-60. Epub 2004 Aug 13. PMID:15310852
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