1u0j
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= REP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Adeno-associated virus 2]) | |GENE= REP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Adeno-associated virus 2]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u0j OCA], [http://www.ebi.ac.uk/pdbsum/1u0j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u0j RCSB]</span> | ||
}} | }} | ||
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[[Category: James, J A.]] | [[Category: James, J A.]] | ||
[[Category: Linden, R M.]] | [[Category: Linden, R M.]] | ||
| - | [[Category: ADP]] | ||
[[Category: aaa+ protein]] | [[Category: aaa+ protein]] | ||
[[Category: helicase]] | [[Category: helicase]] | ||
[[Category: p-loop atpase]] | [[Category: p-loop atpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:03:41 2008'' |
Revision as of 21:03, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | REP (Adeno-associated virus 2) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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