2hcb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2hcb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hcb, resolution 3.51&Aring;" /> '''Structure of AMPPCP-...)
Line 1: Line 1:
-
[[Image:2hcb.gif|left|200px]]<br /><applet load="2hcb" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2hcb.gif|left|200px]]<br /><applet load="2hcb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hcb, resolution 3.51&Aring;" />
caption="2hcb, resolution 3.51&Aring;" />
'''Structure of AMPPCP-bound DnaA from Aquifex aeolicus'''<br />
'''Structure of AMPPCP-bound DnaA from Aquifex aeolicus'''<br />
==Overview==
==Overview==
-
In bacteria, the initiation of replication is controlled by DnaA, a member, of the ATPases associated with various cellular activities (AAA+) protein, superfamily. ATP binding allows DnaA to transition from a monomeric state, into a large oligomeric complex that remodels replication origins, triggers duplex melting and facilitates replisome assembly. The crystal, structure of AMP-PCP-bound DnaA reveals a right-handed superhelix defined, by specific protein-ATP interactions. The observed quaternary structure of, DnaA, along with topology footprint assays, indicates that a right-handed, DNA wrap is formed around the initiation nucleoprotein complex. This model, clarifies how DnaA engages and unwinds bacterial origins and suggests that, additional, regulatory AAA+ proteins engage DnaA at filament ends., Eukaryotic and archaeal initiators also have the structural elements that, promote open-helix formation, indicating that a spiral, open-ring AAA+, assembly forms the core element of initiators in all domains of life.
+
In bacteria, the initiation of replication is controlled by DnaA, a member of the ATPases associated with various cellular activities (AAA+) protein superfamily. ATP binding allows DnaA to transition from a monomeric state into a large oligomeric complex that remodels replication origins, triggers duplex melting and facilitates replisome assembly. The crystal structure of AMP-PCP-bound DnaA reveals a right-handed superhelix defined by specific protein-ATP interactions. The observed quaternary structure of DnaA, along with topology footprint assays, indicates that a right-handed DNA wrap is formed around the initiation nucleoprotein complex. This model clarifies how DnaA engages and unwinds bacterial origins and suggests that additional, regulatory AAA+ proteins engage DnaA at filament ends. Eukaryotic and archaeal initiators also have the structural elements that promote open-helix formation, indicating that a spiral, open-ring AAA+ assembly forms the core element of initiators in all domains of life.
==About this Structure==
==About this Structure==
-
2HCB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with MG and ABG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HCB OCA].
+
2HCB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ABG:'>ABG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HCB OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Berger, J.M.]]
+
[[Category: Berger, J M.]]
-
[[Category: Erzberger, J.P.]]
+
[[Category: Erzberger, J P.]]
-
[[Category: Mott, M.L.]]
+
[[Category: Mott, M L.]]
[[Category: ABG]]
[[Category: ABG]]
[[Category: MG]]
[[Category: MG]]
Line 21: Line 21:
[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:40:08 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:25 2008''

Revision as of 15:40, 21 February 2008


2hcb, resolution 3.51Å

Drag the structure with the mouse to rotate

Structure of AMPPCP-bound DnaA from Aquifex aeolicus

Overview

In bacteria, the initiation of replication is controlled by DnaA, a member of the ATPases associated with various cellular activities (AAA+) protein superfamily. ATP binding allows DnaA to transition from a monomeric state into a large oligomeric complex that remodels replication origins, triggers duplex melting and facilitates replisome assembly. The crystal structure of AMP-PCP-bound DnaA reveals a right-handed superhelix defined by specific protein-ATP interactions. The observed quaternary structure of DnaA, along with topology footprint assays, indicates that a right-handed DNA wrap is formed around the initiation nucleoprotein complex. This model clarifies how DnaA engages and unwinds bacterial origins and suggests that additional, regulatory AAA+ proteins engage DnaA at filament ends. Eukaryotic and archaeal initiators also have the structural elements that promote open-helix formation, indicating that a spiral, open-ring AAA+ assembly forms the core element of initiators in all domains of life.

About this Structure

2HCB is a Single protein structure of sequence from Aquifex aeolicus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling., Erzberger JP, Mott ML, Berger JM, Nat Struct Mol Biol. 2006 Aug;13(8):676-83. Epub 2006 Jul 9. PMID:16829961

Page seeded by OCA on Thu Feb 21 17:40:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools