From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1zvt.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1zvt.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1zvt| PDB=1zvt | SCENE= }} | | {{STRUCTURE_1zvt| PDB=1zvt | SCENE= }} |
| | | | |
| - | '''Structure of the E. coli ParC C-terminal domain'''
| + | ===Structure of the E. coli ParC C-terminal domain=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Most bacteria possess two type IIA topoisomerases, DNA gyrase and topo IV, that together help manage chromosome integrity and topology. Gyrase primarily introduces negative supercoils into DNA, an activity mediated by the C-terminal domain of its DNA binding subunit (GyrA). Although closely related to gyrase, topo IV preferentially decatenates DNA and relaxes positive supercoils. Here we report the structure of the full-length Escherichia coli ParC dimer at 3.0 A resolution. The N-terminal DNA binding region of ParC is highly similar to that of GyrA, but the ParC dimer adopts a markedly different conformation. The C-terminal domain (CTD) of ParC is revealed to be a degenerate form of the homologous GyrA CTD, and is anchored to the top of the N-terminal domains in a configuration different from that thought to occur in gyrase. Biochemical assays show that the ParC CTD controls the substrate specificity of topo IV, likely by capturing DNA segments of certain crossover geometries. This work delineates strong mechanistic parallels between topo IV and gyrase, while explaining how structural differences between the two enzyme families have led to distinct activity profiles. These findings in turn explain how the structures and functions of bacterial type IIA topoisomerases have evolved to meet specific needs of different bacterial families for the control of chromosome superstructure.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16023670}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16023670 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16023670}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| | [[Category: Dna topology]] | | [[Category: Dna topology]] |
| | [[Category: Supercoiling]] | | [[Category: Supercoiling]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:08:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:34:14 2008'' |
Revision as of 17:34, 27 July 2008
Template:STRUCTURE 1zvt
Structure of the E. coli ParC C-terminal domain
Template:ABSTRACT PUBMED 16023670
About this Structure
1ZVT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The structural basis for substrate specificity in DNA topoisomerase IV., Corbett KD, Schoeffler AJ, Thomsen ND, Berger JM, J Mol Biol. 2005 Aug 19;351(3):545-61. PMID:16023670
Page seeded by OCA on Sun Jul 27 20:34:14 2008
