1a3w: Difference between revisions
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[[Image:1a3w.gif|left|200px]] | [[Image:1a3w.gif|left|200px]] | ||
'''PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH FBP, PG, MN2+ AND K+''' | {{Structure | ||
|PDB= 1a3w |SIZE=350|CAPTION= <scene name='initialview01'>1a3w</scene>, resolution 3.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=FBP:FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] | |||
|GENE= | |||
}} | |||
'''PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH FBP, PG, MN2+ AND K+''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A3W is a [ | 1A3W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1A3W with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3W OCA]. | ||
==Reference== | ==Reference== | ||
The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate., Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL, Structure. 1998 Feb 15;6(2):195-210. PMID:[http:// | The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate., Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL, Structure. 1998 Feb 15;6(2):195-210. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9519410 9519410] | ||
[[Category: Pyruvate kinase]] | [[Category: Pyruvate kinase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: tranferase]] | [[Category: tranferase]] | ||
''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 09:52:30 2008'' | ||
Revision as of 10:52, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | , , and | ||||||
| Activity: | Pyruvate kinase, with EC number 2.7.1.40 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH FBP, PG, MN2+ AND K+
OverviewOverview
BACKGROUND: Yeast pyruvate kinase (PK) catalyzes the final step in glycolysis. The enzyme therefore represents an important control point and is allosterically activated by fructose-1,6-bisphosphate (FBP). In mammals the enzyme is found as four different isozymes with different regulatory properties: two of these isozymes are produced by alternate splicing. The allosteric regulation of PK is directly related to proliferation of certain cell types, as demonstrated by the expression of an allosterically regulated isozyme in tumor cells. A model for the allosteric transition from the inactive (T) state to the active (R) state has been proposed previously, but until now the FBP-binding site had not been identified. RESULTS: We report here the structures of PK from yeast complexed with a substrate analog and catalytic metal ions in the presence and absence of bound FBP. The allosteric site is located 40 A from the active site and is entirely located in the enzyme regulatory (C) domain. A phosphate-binding site for the allosteric activator is created by residues encoded by a region of the gene corresponding to the alternately spliced exon of mammalian isozymes. FBP activation appears to induce several conformational changes among active-site sidechains through a mechanism that is most likely to involve significant domain motions, as previously hypothesized. CONCLUSIONS: The structure and location of the allosteric activator site agrees with the pattern of alternate genetic splicing of the PK gene in multicellular eukaryotes that distinguishes between a non-regulated isozyme and the regulated fetal isozymes. The conformational differences observed between the active sites of inactive and fully active PK enzymes is in agreement with the recently determined thermodynamic mechanism of allosteric activation through a 'metal relay' that increases the affinity of the enzyme for its natural phosphoenolpyruvate substrate.
About this StructureAbout this Structure
1A3W is a Single protein structure of sequence from Saccharomyces cerevisiae. The following page contains interesting information on the relation of 1A3W with [The Glycolytic Enzymes]. Full crystallographic information is available from OCA.
ReferenceReference
The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate., Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL, Structure. 1998 Feb 15;6(2):195-210. PMID:9519410
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