2phk: Difference between revisions
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|PDB= 2phk |SIZE=350|CAPTION= <scene name='initialview01'>2phk</scene>, resolution 2.6Å | |PDB= 2phk |SIZE=350|CAPTION= <scene name='initialview01'>2phk</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ATP:ADENOSINE-5 | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphorylase_kinase Phosphorylase kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.19 2.7.11.19] | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphorylase_kinase Phosphorylase kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.19 2.7.11.19] | ||
|GENE= PHKG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]) | |GENE= PHKG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]) | ||
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[[Category: substrate recognition]] | [[Category: substrate recognition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:38:58 2008'' | ||
Revision as of 13:38, 23 March 2008
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| 2phk, resolution 2.6Å | |||||||||||||
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| Ligands: | MN, ATP and GOL | ||||||||||||
| Gene: | PHKG (Oryctolagus cuniculus) | ||||||||||||
| Activity: | Phosphorylase kinase, with EC number 2.7.11.19 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE CRYSTAL STRUCTURE OF A PHOSPHORYLASE KINASE PEPTIDE SUBSTRATE COMPLEX: KINASE SUBSTRATE RECOGNITION
Overview
The structure of a truncated form of the gamma-subunit of phosphorylase kinase (PHKgammat) has been solved in a ternary complex with a non-hydrolysable ATP analogue (adenylyl imidodiphosphate, AMPPNP) and a heptapeptide substrate related in sequence to both the natural substrate and to the optimal peptide substrate. Kinetic characterization of the phosphotransfer reaction confirms the peptide to be a good substrate, and the structure allows identification of key features responsible for its high affinity. Unexpectedly, the substrate peptide forms a short anti-parallel beta-sheet with the kinase activation segment, the region which in other kinases plays an important role in regulation of enzyme activity. This anchoring of the main chain of the substrate peptide at a fixed distance from the gamma-phosphate of ATP explains the selectivity of PHK for serine/threonine over tyrosine as a substrate. The catalytic core of PHK exists as a dimer in crystals of the ternary complex, and the relevance of this phenomenon to its in vivo recognition of dimeric glycogen phosphorylase b is considered.
About this Structure
2PHK is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition., Lowe ED, Noble ME, Skamnaki VT, Oikonomakos NG, Owen DJ, Johnson LN, EMBO J. 1997 Nov 17;16(22):6646-58. PMID:9362479
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