1kzh: Difference between revisions

Revision as of 14:39, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1KZH is a Single protein structure of sequence from Borrelia burgdorferi with as ligand. Active as Diphosphate--fructose-6-phosphate 1-phosphotransferase, with EC number 2.7.1.90 Full crystallographic information is available from OCA.

ReferenceReference

The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi., Moore SA, Ronimus RS, Roberson RS, Morgan HW, Structure. 2002 May;10(5):659-71. PMID:12015149

Page seeded by OCA on Thu Feb 21 13:39:42 2008

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OCA

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-[[Image:1kzh.jpg|left|200px]]<br /><applet load="1kzh" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kzh.jpg|left|200px]]<br /><applet load="1kzh" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kzh, resolution 2.55&Aring;" />
 '''Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi'''<br />
 ==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 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.
 ==About this Structure==
-KZH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Diphosphate--fructose-6-phosphate_1-phosphotransferase Diphosphate--fructose-6-phosphate 1-phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.90 2.7.1.90] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KZH OCA].
+KZH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Diphosphate--fructose-6-phosphate_1-phosphotransferase Diphosphate--fructose-6-phosphate 1-phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.90 2.7.1.90] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZH OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Diphosphate--fructose-6-phosphate 1-phosphotransferase]]
 [[Category: Single protein]]
-[[Category: Moore, S.A.]]
+[[Category: Moore, S A.]]
-[[Category: Morgan, H.W.]]
+[[Category: Morgan, H W.]]
-[[Category: Roberson, R.S.]]
+[[Category: Roberson, R S.]]
-[[Category: Ronimus, R.S.]]
+[[Category: Ronimus, R S.]]
 [[Category: SO4]]
 [[Category: borrelia burgdorferi]]
@@ Line 25: / Line 25: @@
 [[Category: spirochete]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:13:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:42 2008''