2nov: Difference between revisions

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[[Image:2nov.~~gif~~|left|200px]]

[[Image:2nov.png|left|200px]]

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~~'''~~Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target~~'''~~

===Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target===

~~==Overview==~~

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The ~~2.7 A crystal structure of the 55-kDa N-terminal breakage-reunion domain of topoisomerase (topo) IV subunit A (ParC) from Streptococcus pneumoniae~~, the ~~first for~~ the ~~quinolone targets from a gram-positive bacterium, has been solved and reveals a 'closed' dimer similar in fold to Escherichia coli DNA gyrase subunit A~~ (~~GyrA~~), ~~but distinct from the 'open' gate structure of Escherichia coli ParC. Unlike GyrA whose DNA binding groove~~ is ~~largely positively charged, the DNA binding site of ParC exhibits a distinct pattern of alternating positively and negatively charged regions coincident with the predicted positions of~~ the ~~grooves and phosphate backbone of DNA~~. ~~Based on the ParC structure, a new induced~~-~~fit model for sequence~~-specific recognition of the gate (G) segment by ParC has been proposed. These features may account for the unique DNA recognition and quinolone targeting properties of pneumococcal type II topoisomerases compared to their gram-negative counterparts.

The line below this paragraph, {{ABSTRACT_PUBMED_17375187}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17375187 is the PubMed ID number.

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==About this Structure==

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[[Category: Quinolone target]]

[[Category: Topo iv]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 09~~:43:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:59:09 2008''

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-[[Image:2nov.gif|left|200px]]
+{{Seed}}
+[[Image:2nov.png|left|200px]]
 <!--
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 {{STRUCTURE_2nov|  PDB=2nov  |  SCENE=  }}
-'''Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target'''
+===Breakage-reunion domain of S.pneumoniae topo IV: crystal structure of a gram-positive quinolone target===
-==Overview==
+<!--
-The 2.7 A crystal structure of the 55-kDa N-terminal breakage-reunion domain of topoisomerase (topo) IV subunit A (ParC) from Streptococcus pneumoniae, the first for the quinolone targets from a gram-positive bacterium, has been solved and reveals a 'closed' dimer similar in fold to Escherichia coli DNA gyrase subunit A (GyrA), but distinct from the 'open' gate structure of Escherichia coli ParC. Unlike GyrA whose DNA binding groove is largely positively charged, the DNA binding site of ParC exhibits a distinct pattern of alternating positively and negatively charged regions coincident with the predicted positions of the grooves and phosphate backbone of DNA. Based on the ParC structure, a new induced-fit model for sequence-specific recognition of the gate (G) segment by ParC has been proposed. These features may account for the unique DNA recognition and quinolone targeting properties of pneumococcal type II topoisomerases compared to their gram-negative counterparts.
+The line below this paragraph, {{ABSTRACT_PUBMED_17375187}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17375187 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17375187}}
 ==About this Structure==
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 [[Category: Quinolone target]]
 [[Category: Topo iv]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:43:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:59:09 2008''