1bk4: Difference between revisions
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[[Image:1bk4.gif|left|200px]] | [[Image:1bk4.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION''' | {{Structure | ||
|PDB= 1bk4 |SIZE=350|CAPTION= <scene name='initialview01'>1bk4</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BK4 is a [ | 1BK4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BK4 OCA]. | ||
==Reference== | ==Reference== | ||
Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution., Weeks CM, Roszak AW, Erman M, Kaiser R, Jornvall H, Ghosh D, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):93-102. Epub 1999, Jan 1. PMID:[http:// | Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution., Weeks CM, Roszak AW, Erman M, Kaiser R, Jornvall H, Ghosh D, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):93-102. Epub 1999, Jan 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089399 10089399] | ||
[[Category: Fructose-bisphosphatase]] | [[Category: Fructose-bisphosphatase]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
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[[Category: bisphosphatase]] | [[Category: bisphosphatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:06 2008'' |
Revision as of 11:12, 20 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | and | ||||||
Activity: | Fructose-bisphosphatase, with EC number 3.1.3.11 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION
OverviewOverview
The three-dimensional structure of the R form of rabbit liver fructose 1,6-bisphosphatase (Fru-1,6-Pase; E.C. 3.1.3.11) has been determined by a combination of heavy-atom and molecular-replacement methods. A model, which includes 2394 protein atoms and 86 water molecules, has been refined at 2.3 A resolution to a crystallographic R factor of 0.177. The root-mean-square deviations of bond distances and angles from standard geometry are 0.012 A and 1.7 degrees, respectively. This structural result, in conjunction with recently redetermined amino-acid sequence data, unequivocally establishes that the rabbit liver enzyme is not an aberrant bisphosphatase as once believed, but is indeed homologous to other Fru-1,6-Pases. The root-mean-square deviation of the Calpha atoms in the rabbit liver structure from the homologous atoms in the pig kidney structure complexed with the product, fructose 6-phosphate, is 0.7 A. Fru-1,6-Pases are homotetramers, and the rabbit liver protein crystallizes in space group I222 with one monomer in the asymmetric unit. The structure contains a single endogenous Mg2+ ion coordinated by Glu97, Asp118, Asp121 and Glu280 at the site designated metal site 1 in pig kidney Fru-1,6-Pase R-form complexes. In addition, two sulfate ions, which are found at the positions normally occupied by the 6-phosphate group of the substrate, as well as the phosphate of the allosteric inhibitor AMP appear to provide stability. Met177, which has hydrophobic contacts with the adenine moiety of AMP in pig kidney T-form complexes, is replaced by glycine. Binding of a non-hydrolyzable substrate analog, beta-methyl-fructose 1,6-bisphosphate, at the catalytic site is also examined.
About this StructureAbout this Structure
1BK4 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution., Weeks CM, Roszak AW, Erman M, Kaiser R, Jornvall H, Ghosh D, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):93-102. Epub 1999, Jan 1. PMID:10089399
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