1kzh: Difference between revisions

Revision as of 11:21, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kzh.png

Template:STRUCTURE 1kzh

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

Template:ABSTRACT PUBMED 12015149

About this StructureAbout this Structure

1KZH is a Single protein structure of sequence from Borrelia burgdorferi. 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 Wed Jul 2 11:21:45 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1kzh.jpg|left|200px]]
+{{Seed}}
+[[Image:1kzh.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{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==
@@ Line 32: / Line 36: @@
 [[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''