1z5c
From Proteopedia
(New page: 200px<br /><applet load="1z5c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z5c, resolution 2.20Å" /> '''Topoisomerase VI-B, ...) |
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| - | [[Image:1z5c.gif|left|200px]]<br /><applet load="1z5c" size=" | + | [[Image:1z5c.gif|left|200px]]<br /><applet load="1z5c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z5c, resolution 2.20Å" /> | caption="1z5c, resolution 2.20Å" /> | ||
'''Topoisomerase VI-B, ADP Pi bound dimer form'''<br /> | '''Topoisomerase VI-B, ADP Pi bound dimer form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | GHL proteins are functionally diverse enzymes defined by the presence of a | + | GHL proteins are functionally diverse enzymes defined by the presence of a conserved ATPase domain that self-associates to trap substrate upon nucleotide binding. The structural states adopted by these enzymes during nucleotide hydrolysis and product release, and their consequences for enzyme catalysis, have remained unclear. Here, we have determined a complete structural map of the ATP turnover cycle for topoVI-B, the ATPase subunit of the archaeal GHL enzyme topoisomerase VI. With this ensemble of structures, we show that significant conformational changes in the subunit occur first upon ATP binding, and subsequently upon release of hydrolyzed P(i). Together, these data provide a structural framework for understanding the role of ATP hydrolysis in the type II topoisomerase reaction. Our results also suggest that the GHL ATPase module is a molecular switch in which ATP hydrolysis serves as a prerequisite but not a driving force for substrate-dependent structural transitions in the enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_shibatae Sulfolobus shibatae] with MG, PO4 and ADP 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:// | + | 1Z5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_shibatae Sulfolobus shibatae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=ADP:'>ADP</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=1Z5C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus shibatae]] | [[Category: Sulfolobus shibatae]] | ||
| - | [[Category: Berger, J | + | [[Category: Berger, J M.]] |
| - | [[Category: Corbett, K | + | [[Category: Corbett, K D.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: topoisomerase]] | [[Category: topoisomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:20 2008'' |
Revision as of 14:12, 21 February 2008
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Topoisomerase VI-B, ADP Pi bound dimer form
Overview
GHL proteins are functionally diverse enzymes defined by the presence of a conserved ATPase domain that self-associates to trap substrate upon nucleotide binding. The structural states adopted by these enzymes during nucleotide hydrolysis and product release, and their consequences for enzyme catalysis, have remained unclear. Here, we have determined a complete structural map of the ATP turnover cycle for topoVI-B, the ATPase subunit of the archaeal GHL enzyme topoisomerase VI. With this ensemble of structures, we show that significant conformational changes in the subunit occur first upon ATP binding, and subsequently upon release of hydrolyzed P(i). Together, these data provide a structural framework for understanding the role of ATP hydrolysis in the type II topoisomerase reaction. Our results also suggest that the GHL ATPase module is a molecular switch in which ATP hydrolysis serves as a prerequisite but not a driving force for substrate-dependent structural transitions in the enzyme.
About this Structure
1Z5C is a Single protein structure of sequence from Sulfolobus shibatae 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
Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI., Corbett KD, Berger JM, Structure. 2005 Jun;13(6):873-82. PMID:15939019
Page seeded by OCA on Thu Feb 21 16:12:20 2008
