1zxx

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|PDB= 1zxx |SIZE=350|CAPTION= <scene name='initialview01'>1zxx</scene>, resolution 1.85&Aring;
|PDB= 1zxx |SIZE=350|CAPTION= <scene name='initialview01'>1zxx</scene>, resolution 1.85&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </span>
|GENE= pfkA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1585 Lactobacillus delbrueckii subsp. bulgaricus])
|GENE= pfkA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1585 Lactobacillus delbrueckii subsp. bulgaricus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxx OCA], [http://www.ebi.ac.uk/pdbsum/1zxx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zxx RCSB]</span>
}}
}}
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[[Category: Sacchettini, J C.]]
[[Category: Sacchettini, J C.]]
[[Category: Ye, S.]]
[[Category: Ye, S.]]
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[[Category: SO4]]
 
[[Category: allosteric regulation]]
[[Category: allosteric regulation]]
[[Category: lactobacillus bulgaricus]]
[[Category: lactobacillus bulgaricus]]
[[Category: phosphofructokinase]]
[[Category: phosphofructokinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:41:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:43:05 2008''

Revision as of 22:43, 30 March 2008


PDB ID 1zxx

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands:
Gene: pfkA (Lactobacillus delbrueckii subsp. bulgaricus)
Activity: 6-phosphofructokinase, with EC number 2.7.1.11
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The crystal structure of phosphofructokinase from Lactobacillus delbrueckii


Overview

Phosphofructokinase from Lactobacillus delbrueckii subspecies bulgaricus (LbPFK) has been reported to be a nonallosteric analogue of phosphofructokinase from Escherichia coli at pH 8.2 [Le Bras et al. (1991) Eur. J. Biochem. 198, 683-687]. A reexamination of the kinetics of this enzyme shows LbPFK to have limited binding affinity toward the allosteric ligands, MgADP and PEP, with dissociation constants of approximately 20 mM for both. Their allosteric effects are observed only at high concentrations of these ligands, with both exhibiting inhibitory effects on substrate binding. No pH dependence was observed for the binding and the influence of MgADP and PEP on the enzyme. To attempt to explain these results, the crystal structure of LbPFK was solved using molecular replacement to 1.86 A resolution. A comparative study of the LbPFK structure with that of phosphofructokinases from E. coli (EcPFK) and Bacillus stearothermophilus (BsPFK) reveals a structure with conserved fold and substrate binding site. The effector binding site, however, shows many differences that could explain the observed decreases in binding affinity for MgADP and PEP in LbPFK as compared to the other two enzymes.

About this Structure

1ZXX is a Single protein structure of sequence from Lactobacillus delbrueckii subsp. bulgaricus. Full crystallographic information is available from OCA.

Reference

Kinetic and structural characterization of phosphofructokinase from Lactobacillus bulgaricus., Paricharttanakul NM, Ye S, Menefee AL, Javid-Majd F, Sacchettini JC, Reinhart GD, Biochemistry. 2005 Nov 22;44(46):15280-6. PMID:16285731

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