1kzh: Difference between revisions

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[[Image:1kzh.~~jpg~~|left|200px]]

[[Image:1kzh.png|left|200px]]

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~~'''~~Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi~~'''~~

===Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi===

~~==Overview==~~

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The ~~structure of~~ the ~~60 kDa pyrophosphate (PP(i))-dependent phosphofructokinase (PFK) from Borrelia burgdorferi has been solved and refined (R~~(~~free) = 0.243)~~ at 2.~~55 A resolution~~. ~~The domain structure of eubacterial ATP-dependent PFKs~~ is ~~conserved in B. burgdorferi PFK, and there are three large insertions relative to E. coli PFK, including a helical domain containing a hairpin structure that interacts with~~ the ~~active site~~. ~~Asp177, conserved in all PP(i) PFKs, negates the binding of the alpha~~-phosphate group of ATP and likely contacts the essential Mg(2+) cation via a water molecule. Asn181 blocks the binding of the adenine moiety of ATP. Lys203 hydrogen bonds to a sulfate anion that likely mimics PP(i) substrate binding.

The line below this paragraph, {{ABSTRACT_PUBMED_12015149}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12015149 is the PubMed ID number.

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==About this Structure==

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[[Category: Pyrophosphate]]

[[Category: Spirochete]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 23:21:51 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:21:45 2008''

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-[[Image:1kzh.jpg|left|200px]]
+{{Seed}}
+[[Image:1kzh.png|left|200px]]
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 {{STRUCTURE_1kzh|  PDB=1kzh  |  SCENE=  }}
-'''Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi'''
+===Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi===
-==Overview==
+<!--
-The structure of the 60 kDa pyrophosphate (PP(i))-dependent phosphofructokinase (PFK) from Borrelia burgdorferi has been solved and refined (R(free) = 0.243) at 2.55 A resolution. The domain structure of eubacterial ATP-dependent PFKs is conserved in B. burgdorferi PFK, and there are three large insertions relative to E. coli PFK, including a helical domain containing a hairpin structure that interacts with the active site. Asp177, conserved in all PP(i) PFKs, negates the binding of the alpha-phosphate group of ATP and likely contacts the essential Mg(2+) cation via a water molecule. Asn181 blocks the binding of the adenine moiety of ATP. Lys203 hydrogen bonds to a sulfate anion that likely mimics PP(i) substrate binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_12015149}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12015149 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12015149}}
 ==About this Structure==
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 [[Category: Pyrophosphate]]
 [[Category: Spirochete]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:21:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:21:45 2008''