1lii: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1lii |SIZE=350|CAPTION= <scene name='initialview01'>1lii</scene>, resolution 1.73Å | |PDB= 1lii |SIZE=350|CAPTION= <scene name='initialview01'>1lii</scene>, resolution 1.73Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1lij|1LIJ]], [[1lik|1LIK]], [[1lio|1LIO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lii OCA], [http://www.ebi.ac.uk/pdbsum/1lii PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lii RCSB]</span> | |||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Scott, D M.]] | [[Category: Scott, D M.]] | ||
[[Category: Ullman, B.]] | [[Category: Ullman, B.]] | ||
[[Category: alpha-beta structure]] | [[Category: alpha-beta structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:03:15 2008'' | ||
Revision as of 22:03, 30 March 2008
| |||||||
| , resolution 1.73Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Adenosine kinase, with EC number 2.7.1.20 | ||||||
| Related: | 1LIJ, 1LIK, 1LIO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE 2 AND AMP-PCP
OverviewOverview
Adenosine kinase (AK) is a key purine metabolic enzyme from the opportunistic parasitic protozoan Toxoplasma gondii and belongs to the family of carbohydrate kinases that includes ribokinase. To understand the catalytic mechanism of AK, we determined the structures of the T. gondii apo AK, AK:adenosine complex and the AK:adenosine:AMP-PCP complex to 2.55 A, 2.50 A and 1.71 A resolution, respectively. These structures reveal a novel catalytic mechanism that involves an adenosine-induced domain rotation of 30 degrees and a newly described anion hole (DTXGAGD), requiring a helix-to-coil conformational change that is induced by ATP binding. Nucleotide binding also evokes a coil-to-helix transition that completes the formation of the ATP binding pocket. A conserved dipeptide, Gly68-Gly69, which is located at the bottom of the adenosine-binding site, functions as the switch for domain rotation. The synergistic structural changes that occur upon substrate binding sequester the adenosine and the ATP gamma phosphate from solvent and optimally position the substrates for catalysis. Finally, the 1.84 A resolution structure of an AK:7-iodotubercidin:AMP-PCP complex reveals the basis for the higher affinity binding of this prodrug over adenosine and thus provides a scaffold for the design of new inhibitors and subversive substrates that target the T. gondii AK.
About this StructureAbout this Structure
1LII is a Single protein structure of sequence from Toxoplasma gondii. This structure supersedes the now removed PDB entry 1DGY. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding., Schumacher MA, Scott DM, Mathews II, Ealick SE, Roos DS, Ullman B, Brennan RG, J Mol Biol. 2000 May 19;298(5):875-93. PMID:10801355
Page seeded by OCA on Sun Mar 30 22:03:15 2008