1kij
From Proteopedia
(New page: 200px<br /><applet load="1kij" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kij, resolution 2.30Å" /> '''Crystal structure of...) |
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| - | [[Image:1kij.gif|left|200px]]<br /><applet load="1kij" size=" | + | [[Image:1kij.gif|left|200px]]<br /><applet load="1kij" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kij, resolution 2.30Å" /> | caption="1kij, resolution 2.30Å" /> | ||
'''Crystal structure of the 43K ATPase domain of Thermus thermophilus gyrase B in complex with novobiocin'''<br /> | '''Crystal structure of the 43K ATPase domain of Thermus thermophilus gyrase B in complex with novobiocin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | DNA gyrase forms an A(2)B(2) tetramer involved in DNA replication, repair, recombination, and transcription in which the B subunit catalyzes ATP | + | DNA gyrase forms an A(2)B(2) tetramer involved in DNA replication, repair, recombination, and transcription in which the B subunit catalyzes ATP hydrolysis. The Thermus thermophilus and Escherichia coli gyrases are homologues and present the same catalytic activity. When compared with that of the E. coli 43K-5'-adenylyl-beta,gamma-imidodiphosphate complex, the crystal structure of Gyrase B 43K ATPase domain in complex with novobiocin, one of the most potent inhibitors of gyrase shows large conformational changes of the subdomains within the dimer. The stabilization of loop 98-118 closing the active site through dimeric contacts and interaction with domain 2 allows to observe novobiocin-protein interactions that could not be seen in the 24K-inhibitor complexes. Furthermore, this loop adopts a position which defines an "open" conformation of the active site in absence of ATP, in contrast with the "closed" conformation adopted upon ATP binding. All together, these results indicate how the subdomains may propagate conformational changes from the active site and provide crucial information for the design of more specific inhibitors. |
==About this Structure== | ==About this Structure== | ||
| - | 1KIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with NOV and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http:// | + | 1KIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=NOV:'>NOV</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Hoermann, L.]] | [[Category: Hoermann, L.]] | ||
| - | [[Category: Jeltsch, J | + | [[Category: Jeltsch, J M.]] |
[[Category: Lamour, V.]] | [[Category: Lamour, V.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
| Line 24: | Line 24: | ||
[[Category: topoisomerase]] | [[Category: topoisomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:31 2008'' |
Revision as of 11:34, 21 February 2008
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Crystal structure of the 43K ATPase domain of Thermus thermophilus gyrase B in complex with novobiocin
Overview
DNA gyrase forms an A(2)B(2) tetramer involved in DNA replication, repair, recombination, and transcription in which the B subunit catalyzes ATP hydrolysis. The Thermus thermophilus and Escherichia coli gyrases are homologues and present the same catalytic activity. When compared with that of the E. coli 43K-5'-adenylyl-beta,gamma-imidodiphosphate complex, the crystal structure of Gyrase B 43K ATPase domain in complex with novobiocin, one of the most potent inhibitors of gyrase shows large conformational changes of the subdomains within the dimer. The stabilization of loop 98-118 closing the active site through dimeric contacts and interaction with domain 2 allows to observe novobiocin-protein interactions that could not be seen in the 24K-inhibitor complexes. Furthermore, this loop adopts a position which defines an "open" conformation of the active site in absence of ATP, in contrast with the "closed" conformation adopted upon ATP binding. All together, these results indicate how the subdomains may propagate conformational changes from the active site and provide crucial information for the design of more specific inhibitors.
About this Structure
1KIJ is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Active as DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 Full crystallographic information is available from OCA.
Reference
An open conformation of the Thermus thermophilus gyrase B ATP-binding domain., Lamour V, Hoermann L, Jeltsch JM, Oudet P, Moras D, J Biol Chem. 2002 May 24;277(21):18947-53. Epub 2002 Feb 15. PMID:11850422
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