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1kzh
From Proteopedia
(New page: 200px<br /><applet load="1kzh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kzh, resolution 2.55Å" /> '''Structure of a pyrop...) |
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| - | [[Image:1kzh.jpg|left|200px]]<br /><applet load="1kzh" size=" | + | [[Image:1kzh.jpg|left|200px]]<br /><applet load="1kzh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kzh, resolution 2.55Å" /> | caption="1kzh, resolution 2.55Å" /> | ||
'''Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi'''<br /> | '''Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the 60 kDa pyrophosphate (PP(i))-dependent | + | 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== | ==About this Structure== | ||
| - | 1KZH 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:// | + | 1KZH 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== | ==Reference== | ||
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[[Category: Diphosphate--fructose-6-phosphate 1-phosphotransferase]] | [[Category: Diphosphate--fructose-6-phosphate 1-phosphotransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Moore, S | + | [[Category: Moore, S A.]] |
| - | [[Category: Morgan, H | + | [[Category: Morgan, H W.]] |
| - | [[Category: Roberson, R | + | [[Category: Roberson, R S.]] |
| - | [[Category: Ronimus, R | + | [[Category: Ronimus, R S.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: borrelia burgdorferi]] | [[Category: borrelia burgdorferi]] | ||
| Line 25: | Line 25: | ||
[[Category: spirochete]] | [[Category: spirochete]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:42 2008'' |
Revision as of 11:39, 21 February 2008
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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.
About 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.
Reference
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
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