6pfk: Difference between revisions
New page: left|200px<br /> <applet load="6pfk" size="450" color="white" frame="true" align="right" spinBox="true" caption="6pfk, resolution 2.6Å" /> '''PHOSPHOFRUCTOKINASE,... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:6pfk.gif|left|200px]]<br /> | [[Image:6pfk.gif|left|200px]]<br /><applet load="6pfk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="6pfk" size=" | |||
caption="6pfk, resolution 2.6Å" /> | caption="6pfk, resolution 2.6Å" /> | ||
'''PHOSPHOFRUCTOKINASE, INHIBITED T-STATE'''<br /> | '''PHOSPHOFRUCTOKINASE, INHIBITED T-STATE'''<br /> | ||
==Overview== | ==Overview== | ||
Comparison between the crystal structures of low- and high-affinity forms | Comparison between the crystal structures of low- and high-affinity forms of phosphofructokinase shows a close coupling between the change of quaternary structure and local changes triggered by binding of the allosteric effectors. These concerted changes link all the substrate and effector sites in the tetramer, and explain the change of affinity for the cooperative substrate. | ||
==About this Structure== | ==About this Structure== | ||
6PFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with PGA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | 6PFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=PGA:'>PGA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 5PFK. The following page contains interesting information on the relation of 6PFK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PFK OCA]. | ||
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: The Glycolytic Enzymes]] | [[Category: The Glycolytic Enzymes]] | ||
[[Category: Auer, M.]] | [[Category: Auer, M.]] | ||
[[Category: Evans, P | [[Category: Evans, P R.]] | ||
[[Category: Schirmer, T.]] | [[Category: Schirmer, T.]] | ||
[[Category: PGA]] | [[Category: PGA]] | ||
| Line 24: | Line 23: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:16:40 2008'' | ||
Revision as of 20:16, 21 February 2008
|
PHOSPHOFRUCTOKINASE, INHIBITED T-STATE
OverviewOverview
Comparison between the crystal structures of low- and high-affinity forms of phosphofructokinase shows a close coupling between the change of quaternary structure and local changes triggered by binding of the allosteric effectors. These concerted changes link all the substrate and effector sites in the tetramer, and explain the change of affinity for the cooperative substrate.
About this StructureAbout this Structure
6PFK is a Single protein structure of sequence from Geobacillus stearothermophilus with as ligand. This structure supersedes the now removed PDB entry 5PFK. The following page contains interesting information on the relation of 6PFK with [The Glycolytic Enzymes]. Active as 6-phosphofructokinase, with EC number 2.7.1.11 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of the allosteric behaviour of phosphofructokinase., Schirmer T, Evans PR, Nature. 1990 Jan 11;343(6254):140-5. PMID:2136935
Page seeded by OCA on Thu Feb 21 19:16:40 2008