2f4q
From Proteopedia
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| - | [[Image:2f4q.gif|left|200px]] | + | [[Image:2f4q.gif|left|200px]] |
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| - | '''Crystal Structure of Deinococcus radiodurans topoisomerase IB''' | + | {{Structure |
| + | |PDB= 2f4q |SIZE=350|CAPTION= <scene name='initialview01'>2f4q</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= TopIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 Deinococcus radiodurans]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Deinococcus radiodurans topoisomerase IB''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F4Q is a [ | + | 2F4Q is a [[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=2F4Q OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a bacterial type IB DNA topoisomerase reveals a preassembled active site in the absence of DNA., Patel A, Shuman S, Mondragon A, J Biol Chem. 2006 Mar 3;281(9):6030-7. Epub 2005 Dec 19. PMID:[http:// | + | Crystal structure of a bacterial type IB DNA topoisomerase reveals a preassembled active site in the absence of DNA., Patel A, Shuman S, Mondragon A, J Biol Chem. 2006 Mar 3;281(9):6030-7. Epub 2005 Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16368685 16368685] |
[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: topoisomerase ib]] | [[Category: topoisomerase ib]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:48:04 2008'' |
Revision as of 14:48, 20 March 2008
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| , resolution 1.75Å | |||||||
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| Gene: | TopIB (Deinococcus radiodurans) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Deinococcus radiodurans topoisomerase IB
Overview
Type IB DNA topoisomerases are found in all eukarya, two families of eukaryotic viruses (poxviruses and mimivirus), and many genera of bacteria. They alter DNA topology by cleaving and resealing one strand of duplex DNA via a covalent DNA-(3-phosphotyrosyl)-enzyme intermediate. Bacterial type IB enzymes were discovered recently and are described as poxvirus-like with respect to their small size, primary structures, and bipartite domain organization. Here we report the 1.75-A crystal structure of Deinococcus radiodurans topoisomerase IB (DraTopIB), a prototype of the bacterial clade. DraTopIB consists of an amino-terminal (N) beta-sheet domain (amino acids 1-90) and a predominantly alpha-helical carboxyl-terminal (C) domain (amino acids 91-346) that closely resemble the corresponding domains of vaccinia virus topoisomerase IB. The five amino acids of DraTopIB that comprise the catalytic pentad (Arg-137, Lys-174, Arg-239, Asn-280, and Tyr-289) are preassembled into the active site in the absence of DNA in a manner nearly identical to the pentad configuration in human topoisomerase I bound to DNA. This contrasts with the apoenzyme of vaccinia topoisomerase, in which three of the active site constituents are either displaced or disordered. The N and C domains of DraTopIB are splayed apart in an "open" conformation, in which the surface of the catalytic domain containing the active site is exposed for DNA binding. A comparison with the human topoisomerase I-DNA cocrystal structure suggests how viral and bacterial topoisomerase IB enzymes might bind DNA circumferentially via movement of the N domain into the major groove and clamping of a disordered loop of the C domain around the helix.
About this Structure
2F4Q is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
Crystal structure of a bacterial type IB DNA topoisomerase reveals a preassembled active site in the absence of DNA., Patel A, Shuman S, Mondragon A, J Biol Chem. 2006 Mar 3;281(9):6030-7. Epub 2005 Dec 19. PMID:16368685
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